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Information on EC 7.2.2.14 - P-type Mg2+ transporter
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7.2.2.14 P-type Mg2+ transporterIUBMB Comments
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. A bacterial enzyme that imports Mg2+ with, rather than against, the Mg2+ electrochemical gradient. The enzyme is also involved in Ni2+ import.
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Word Map
- 7.2.2.14
- na+
- atpases
- triphosphatase
- mg2+-atpase
-
sarcoplasmic
-
ca2+-stimulated
-
submitochondrial
- ouabain
-
sarcolemmal
- myofibrillar
-
amelogenesis
-
hypomagnesemia
- medicine
- imperfecta
- actomyosin
-
cone-rode
-
actin-activated
-
oligomycin-insensitive
-
ouabain-sensitive
- dicyclohexylcarbodiimide
-
atp-driven
- ecto-atpase
- n,n'-dicyclohexylcarbodiimide
-
melastatin
-
3.6.1.3
- synthesis
- biotechnology
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
mg2+ atpase, mg2+-dependent atpase, magt1, slc41a1, oligomycin-sensitive atpase, magnesium transporter, cnnm4, mg2+ transporter, mrs2p, mrs2-4, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
adenosine 5'-triphosphatase
-
-
-
-
adenosine triphosphatase
-
-
-
-
ALR1
ATP hydrolase
-
-
-
-
ATP phosphohydrolase
-
-
-
-
ATPase
-
-
-
-
complex V (mitochondrial electron transport)
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-
-
-
CorA
EC 3.6.3.2
-
-
formerly
-
magnesium transporter
Mg2+ transporter
Mg2+-ATPase
Mg2+-dependent ATPase
Mg2+-transporting P-type ATPase
MgtA
MgtA Mg2+ transporter
MgtB
MgtC
MgtE
Mrs2p
additional information
additional information
-
the enzymes belong to the MGT gene family, i.e. MRS2
additional information
-
the enzyme belongs to the 2-TM-GxN family of Mg2+ transporters
additional information
the enzyme belongs to the 2-TM-GxN family of Mg2+ transporters
additional information
the enzyme belongs to the 2-TM-GxN family of Mg2+ transporters
additional information
the enzyme belongs to the Mrs2 protein family
additional information
the enzyme is a member of the CorA-Mrs2-Alr1 superfamily of Mg21 transporters
additional information
the enzyme belongs to the 2-TM-GxN family of Mg2+ transporters
additional information
the enzyme is a member of the CorA-Mrs2-Alr1 superfamily of Mg21 transporters
-
additional information
-
MgtA/B transporters belong to the P-type ATPase superfamily
additional information
-
the enzyme belongs to the CorA Mg2+ transporter superfamily
additional information
the enzyme belongs to the 2-TM-GxN family of Mg2+ transporters
additional information
the enzyme belongs to the CorA-Alr1-Mrs2 superfamily
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + Mg2+[side 1] = ADP + phosphate + Mg2+[side 2]
-
-
-
-
ATP + H2O + Mg2+[side 1] = ADP + phosphate + Mg2+[side 2]
a 10-member Arabidopsis gene family, AtMGT for Arabidopsis thaliana magnesium transport, encodes a Mg2+ transport system, CorA-like proteins.
-
ATP + H2O + Mg2+[side 1] = ADP + phosphate + Mg2+[side 2]
Three distinct families of prokaryotic Mg2+ transport proteins have been identified and cloned: MgtE, CorA and MgtA/B. MgtA/B class of Mg2+ transporter are P-type ATPases.
-
ATP + H2O + Mg2+[side 1] = ADP + phosphate + Mg2+[side 2]
Three transporters mediate Mg2+-uptake, the P-type ATPases MgtA and MgtB, whose expression is transcriptionally induced in low Mg2+ by the Mg2+-regulated PhoP/PhoQ two-component system, and CorA, whose transcription is regulated neither by the levels of Mg2+ nor by the PhoP/PhoQ system. CorA modulates its activity in response to the presence of PhoP-regulated gene products.
-
ATP + H2O + Mg2+[side 1] = ADP + phosphate + Mg2+[side 2]
efflux system is mediated by a ring of conserved aspartic residues at the cytoplasmic entrance and a carbonyl funnel at the periplasmic side of the pore
-
ATP + H2O + Mg2+[side 1] = ADP + phosphate + Mg2+[side 2]
Mg2+ transport involves first the binding of the fully hydrated ion to an extracellular binding loop connecting the transmembrane domain, passage through the membrane, not involving electrostatic interactions but two cytsolic domains, one with extremely high positive charges and the other with negative charge helping to control the Mg2+ flux in concert with an intracellular Mg2+ bound between the domains of each monomer, transport mechanism, overview
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ATP + H2O + Mg2+[side 1] = ADP + phosphate + Mg2+[side 2]
Mg2+ transport involves first the binding of the fully hydrated ion to an extracellular binding loop connecting the transmembrane domain, passage through the membrane, not involving electrostatic interactions but two cytsolic domains, one with extremely high positive charges and the other with negative charge helping to control the Mg2+ flux in concert with an intracellular Mg2+ bound between the domains of each monomer, transport mechanism, overview
-
ATP + H2O + Mg2+[side 1] = ADP + phosphate + Mg2+[side 2]
Mg2+ transport involves first the binding of the fully hydrated ion to an extracellular binding loop connecting the transmembrane domain, passage through the membrane, not involving electrostatic interactions but two cytsolic domains, one with extremely high positive charges and the other with negative charge helping to control the Mg2+ flux in concert with an intracellular Mg2+ bound between the domains of each monomer, transport mechanism, overview
-
ATP + H2O + Mg2+[side 1] = ADP + phosphate + Mg2+[side 2]
Mg2+ transport involves first the binding of the fully hydrated ion to an extracellular binding loop connecting the transmembrane domain, passage through the membrane, not involving electrostatic interactions but two cytsolic domains, one with extremely high positive charges and the other with negative charge helping to control the Mg2+ flux in concert with an intracellular Mg2+ bound between the domains of each monomer, transport mechanism, overview
-
ATP + H2O + Mg2+[side 1] = ADP + phosphate + Mg2+[side 2]
Mg2+ transport involves first the binding of the fully hydrated ion to an extracellular binding loop connecting the transmembrane domain, passage through the membrane, not involving electrostatic interactions but two cytsolic domains, one with extremely high positive charges and the other with negative charge helping to control the Mg2+ flux in concert with an intracellular Mg2+ bound between the domains of each monomer, transport mechanism, overview
-
ATP + H2O + Mg2+[side 1] = ADP + phosphate + Mg2+[side 2]
Mg2+ transport involves first the binding of the fully hydrated ion to an extracellular binding loop connecting the transmembrane domain, passage through the membrane, not involving electrostatic interactions but two cytsolic domains, one with extremely high positive charges and the other with negative charge helping to control the Mg2+ flux in concert with an intracellular Mg2+ bound between the domains of each monomer, transport mechanism, overview
-
ATP + H2O + Mg2+[side 1] = ADP + phosphate + Mg2+[side 2]
Mg2+ transport involves first the binding of the fully hydrated ion to an extracellular binding loop connecting the transmembrane domain, passage through the membrane, not involving electrostatic interactions but two cytsolic domains, one with extremely high positive charges and the other with negative charge helping to control the Mg2+ flux in concert with an intracellular Mg2+ bound between the domains of each monomer, transport mechanism, overview
-
ATP + H2O + Mg2+[side 1] = ADP + phosphate + Mg2+[side 2]
Mg2+ transport involves first the binding of the fully hydrated ion to an extracellular binding loop connecting the transmembrane domain, passage through the membrane, not involving electrostatic interactions but two cytsolic domains, one with extremely high positive charges and the other with negative charge helping to control the Mg2+ flux in concert with an intracellular Mg2+ bound between the domains of each monomer, transport mechanism, overview
-
ATP + H2O + Mg2+[side 1] = ADP + phosphate + Mg2+[side 2]
Mg2+ transport involves first the binding of the fully hydrated ion to an extracellular binding loop connecting the transmembrane domain, passage through the membrane, not involving electrostatic interactions but two cytsolic domains, one with extremely high positive charges and the other with negative charge helping to control the Mg2+ flux in concert with an intracellular Mg2+ bound between the domains of each monomer, transport mechanism, overview
ATP + H2O + Mg2+[side 1] = ADP + phosphate + Mg2+[side 2]
Mg2+ transport involves first the binding of the fully hydrated ion to an extracellular binding loop connecting the transmembrane domain, passage through the membrane, not involving electrostatic interactions but two cytsolic domains, one with extremely high positive charges and the other with negative charge helping to control the Mg2+ flux in concert with an intracellular Mg2+ bound between the domains of each monomer, transport mechanism, overview
-
ATP + H2O + Mg2+[side 1] = ADP + phosphate + Mg2+[side 2]
Mg2+ transport involves first the binding of the fully hydrated ion to an extracellular binding loop connecting the transmembrane domain, passage through the membrane, not involving electrostatic interactions but two cytsolic domains, one with extremely high positive charges and the other with negative charge helping to control the Mg2+ flux in concert with an intracellular Mg2+ bound between the domains of each monomer, transport mechanism, overview
ATP + H2O + Mg2+[side 1] = ADP + phosphate + Mg2+[side 2]
Mg2+ transport mechanism, structure-function relationship, overview
ATP + H2O + Mg2+[side 1] = ADP + phosphate + Mg2+[side 2]
Mg2+ transport involves first the binding of the fully hydrated ion to an extracellular binding loop connecting the transmembrane domain, passage through the membrane, not involving electrostatic interactions but two cytsolic domains, one with extremely high positive charges and the other with negative charge helping to control the Mg2+ flux in concert with an intracellular Mg2+ bound between the domains of each monomer, transport mechanism, overview
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
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-
-
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transmembrane transport
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-
-
-
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (P-type, Mg2+-importing)
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. A bacterial enzyme that imports Mg2+ with, rather than against, the Mg2+ electrochemical gradient. The enzyme is also involved in Ni2+ import.
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CAS REGISTRY NUMBER
COMMENTARY
9000-83-3
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + H2O + Co2+/in
ADP + phosphate + Co2+/out
-
apparent dissociation constant: wild-type, 0.0298 mM, recombinant periplasmic domain, 0.0236 mM
-
-
?
ATP + H2O + Mg2+/in
ADP + phosphate + Mg2+/out
-
apparent dissociation constant: wild-type, 0.0184 mM, recombinant periplasmic domain, 0.0309 mM9
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-
?
ATP + H2O + Co2+/out
ADP + phosphate + Co2+/in
-
-
-
-
?
ATP + H2O + Co2+/out
ADP + phosphate + Co2+/in
-
transported by CorA
-
-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
-
MGT9 functions as a low-affinity Mg2+-transporter, is essential for pollen development, and plays a critical role in many physiological processes
-
-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
-
MGT9 is capable of mediating Mg2+ uptake in the sub-millimolar range
-
-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
-
Mrs2 is the major transport protein for Mg2+ uptake into mitochondria, and expression of Mrs2 is essential for the maintenance of respiratory complex I and cell viability
-
-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
-
Mg2+ regulates the entry of Ni2+ ions playing a protective role to minimize Ni2+ toxicity
-
-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
-
Mg2+ regulates the entry of Ni2+ ions
-
-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
-
Mg2+ regulates the entry of Ni2+ ions playing a protective role to minimize Ni2+ toxicity
-
-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
-
Mg2+ regulates the entry of Ni2+ ions
-
-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
-
a choline depriving diet increases the enzyme levels in hippocampus, cerebellum, and pons of male rat brains by 19-85%, Mg2+-ATPase is induced by choline deprivation
-
-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
-
-
-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
-
-
-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
-
isoform Alr2p contributes poorly to uptake of Mg2+
-
-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
at high Mg2+ levels Alr1p is rapidly degraded by the ubiquitin dependent pathway
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-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
Mg2+ uptake by Mrs2p is functionally regulated in the mitochondria
-
-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
Mrs2 protein forms a Mg2+-selective channel of high conductance, which has an open probability of about 60% in the absence of Mg2+ at the matrix site, that decreases to about 20% in its presence, the selective channel controls Mg2+ influx into mitochondria by an intrinsic negative feedback mechanism
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-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
-
-
-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
Mrs2 protein forms a Mg2+-selective channel of high conductance, which has an open probability of about 60% in the absence of Mg2+ at the matrix site, that decreases to about 20% in its presence, the selective channel controls Mg2+ influx into mitochondria by an intrinsic negative feedback mechanism
-
-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
-
the MgtC is a virulence factor in Salmonella Typhimurium that is required for growth at low Mg2+ concentrations and intramacrophage survival
-
-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
-
-
-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
-
-
-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
-
-
-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
-
-
-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
-
-
-
-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
-
-
-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
-
-
-
-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
-
CorA and MgtE are not transcriptionally regulated
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-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
-
transported by CorA, MgtA, and MgtB
-
-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
-
-
-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
-
a fully hydrated Mg2+ binds in the periplasm, interaction of CprA with Mg2+ and transport mechanism, overview
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-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
CorA contains an unusually long ion pore putatively gated by hydrophobic residues near the intracellular end and by universally conserved asparagine residues at the periplasmic entrance, structure-function relationships and gating mechanisms in the CorA Mg2+ transport system, the intracellular funnel domain constitutes an allosteric regulatory module that can be engineered to promote an activated or closed state, involvement of the alpha5 and alpha6 helices in CorA function, overview
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-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
One metal binds near the universally conserved GMN motif, apparently stabilized within the transmembrane region discriminating between the size and preferred coordination geometry of hydrated substrates. CorA achieves specificity by requiring the sequential dehydration of substrates. Ten metal sites are located within the cytoplasmic funnel domain and linked to long extensions of the pore helices regulating the transport status of CorA, this region is an intrinsic divalent cation sensor functioning as a Mg2+-specific homeostatic molecular switch, overview
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-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
Mg21 homeostasis mechanism model, overview
-
-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
transport of the fully hydrated Mg2+ ion, one Mg2+ is bound to conserved Asp432 within the solvent-accessible pore of the transmembrane segement, four Mg2+ ions are bound at the interface between the connecting helices and the other domains, Mg2+ binding structure, overview
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-
?
ATP + H2O + Ni2+/in
ADP + phosphate + Ni2+/out
-
apparent dissociation constant: wild-type, 0.201 mM, recombinant periplasmic domain, 0.106 mM
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-
?
ATP + H2O + Ni2+/out
ADP + phosphate + Ni2+/in
-
Mg2+ and Zn2+ regulate the entry of Ni2+ ions
-
-
?
ATP + H2O + Ni2+/out
ADP + phosphate + Ni2+/in
-
Mg2+ and Zn2+ regulate the entry of Ni2+ ions
-
-
?
ATP + H2O + Ni2+/out
ADP + phosphate + Ni2+/in
-
-
-
?
ATP + H2O + Ni2+/out
ADP + phosphate + Ni2+/in
-
-
-
?
ATP + H2O + Ni2+/out
ADP + phosphate + Ni2+/in
-
-
-
-
?
ATP + H2O + Ni2+/out
ADP + phosphate + Ni2+/in
-
transported by CorA, MgtA, and MgtB
-
-
?
additional information
?
-
-
The AtMGT family of transports is involved in Mg2+ transport acquisition from the environment and/or in Mg2+ transport within the plant.
-
-
?
additional information
?
-
-
Different AtMGT members have different cation selectivity that contributes to the functional diversity of the protein family. AtMGT1 may transport Mg2+ with the highest efficiency of all the divalent cations tested: Cu2+ Fe2+ Mn2+, Co2+ Cd2+, Mg2+.
-
-
?
additional information
?
-
-
the Arabidopsis thaliana CorA homologues of the Mrs2p family have putative transmembrane segments and catalyzes Mg2+ transport, CorA does not contain an ATP binding site and acts as a Mg2+ channel probably driven by the inward electrochemical Mg2+ potential
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-
?
additional information
?
-
-
CorA does not contain an ATP binding site and acts as a Mg2+ channel probably driven by the inward electrochemical Mg2+ potential
-
-
?
additional information
?
-
CorA does not contain an ATP binding site and acts as a Mg2+ channel probably driven by the inward electrochemical Mg2+ potential
-
-
?
additional information
?
-
-
the enzyme activity in slightly increased in diabetic rats. Seasonal differences in Mg2+-ATPase activity may play a decisive role in the evaluation of properties and function of rat heart mitochondria, overview
-
-
?
additional information
?
-
-
the enzyme activity is increased in isoprenaline-induced myocardial infarcted rats
-
-
?
additional information
?
-
with lower conductance, the Mrs2 channel is also permeable for Ni2+, whereas no permeability has been observed for either Ca2+, Mn2+, or Co2+
-
-
?
additional information
?
-
-
Lpe10p modulates the conductance of the enzyme channel. The interplay of Lpe10p and enzyme Mrs2p is of central significance for the transport of Mg2+ into mitochondria of Saccharomyces cerevisiae
-
-
?
additional information
?
-
-
Lpe10p modulates the conductance of the enzyme channel. The interplay of Lpe10p and enzyme Mrs2p is of central significance for the transport of Mg2+ into mitochondria of Saccharomyces cerevisiae
-
-
?
additional information
?
-
with lower conductance, the Mrs2 channel is also permeable for Ni2+, whereas no permeability has been observed for either Ca2+, Mn2+, or Co2+
-
-
?
additional information
?
-
-
CorA does not contain an ATP binding site and acts as a Mg2+ channel probably driven by the inward electrochemical Mg2+ potential, the different cation influx activities do not influence each other activity, MgtA and MgtB are P-type ATPases
-
-
?
additional information
?
-
-
no transport of Fe2+, Mn2+, or Ca2+
-
-
?
additional information
?
-
CorA does not contain an ATP binding site and acts as a Mg2+ channel probably driven by the inward electrochemical Mg2+ potential
-
-
?
additional information
?
-
CorA is selective for magnesium ions over calcium ions with a 100fold greater uptake rate
-
-
?
additional information
?
-
-
the CorA monomer has a C-terminal membrane domain containing two transmembrane segments, and a large, highly negatively charged N-terminal cytoplasmic soluble domain, the enzyme forms a homopentamer shaped like a funnel with Asn314 at the entrance, which interacts with the ring of positive charges external to the ion conduction pathwayat the cytosolicmembrane interface, in the membrane
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
-
MGT9 functions as a low-affinity Mg2+-transporter, is essential for pollen development, and plays a critical role in many physiological processes
-
-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
-
Mrs2 is the major transport protein for Mg2+ uptake into mitochondria, and expression of Mrs2 is essential for the maintenance of respiratory complex I and cell viability
-
-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
-
Mg2+ regulates the entry of Ni2+ ions playing a protective role to minimize Ni2+ toxicity
-
-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
-
Mg2+ regulates the entry of Ni2+ ions playing a protective role to minimize Ni2+ toxicity
-
-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
-
a choline depriving diet increases the enzyme levels in hippocampus, cerebellum, and pons of male rat brains by 19-85%, Mg2+-ATPase is induced by choline deprivation
-
-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
-
-
-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
-
-
-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
at high Mg2+ levels Alr1p is rapidly degraded by the ubiquitin dependent pathway
-
-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
Mg2+ uptake by Mrs2p is functionally regulated in the mitochondria
-
-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
-
-
-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
-
the MgtC is a virulence factor in Salmonella Typhimurium that is required for growth at low Mg2+ concentrations and intramacrophage survival
-
-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
-
-
-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
-
-
-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
-
-
-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
-
-
-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
-
-
-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
-
-
-
-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
-
CorA and MgtE are not transcriptionally regulated
-
-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
-
-
-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
Mg21 homeostasis mechanism model, overview
-
-
?
ATP + H2O + Ni2+/out
ADP + phosphate + Ni2+/in
-
Mg2+ and Zn2+ regulate the entry of Ni2+ ions
-
-
?
ATP + H2O + Ni2+/out
ADP + phosphate + Ni2+/in
-
Mg2+ and Zn2+ regulate the entry of Ni2+ ions
-
-
?
additional information
?
-
-
The AtMGT family of transports is involved in Mg2+ transport acquisition from the environment and/or in Mg2+ transport within the plant.
-
-
?
additional information
?
-
-
the enzyme activity in slightly increased in diabetic rats. Seasonal differences in Mg2+-ATPase activity may play a decisive role in the evaluation of properties and function of rat heart mitochondria, overview
-
-
?
additional information
?
-
-
the enzyme activity is increased in isoprenaline-induced myocardial infarcted rats
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
additional information
-
no or poor inhibition of CorA by Ca2+, Sr2+, Ba2+, Zn2+, Fe2+, and Fe3+
Mg2+
the enzyme is activated when the free Mg2+ concentration is reduced below 0.01 mM
Mg2+
a significant part of the selectivity for Mg2+ derives from binding the fully hydrated cation
Mg2+
-
-
Mg2+
-
bound between enzyme subunits at a conserved site in the cytoplasmic domain
Mg2+
-
dependent on. The ATPase activity is abolished in absence of ATP and Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cetyltrimethylammonium bromide
-
Mg2+-ATPase activity of ECF1 is very resistant to inhibition by cationic detergents melittin and cetyltrimethylammonium bromide, lower concentrations of cetyltrimethylammonium bromide stimulate Mg2+-ATPase activity of ECF1. MgATP protects, overview
Co(III) hexaamines
inhibit Mrs2p and CorA, inhibition of Ni2+ uptake by CorA
-
cysteine
-
inhibits the Mg2+-ATPase activity by 15%, in addition with lanthanum by 25%
lanthanum
-
inhibits the Mg2+-ATPase activity by 8%, not reversible but increased by Cys co-administration to 25% inhibition
ruthenium (III) hexaamines
inhibit Mrs2p and CorA, inhibition of Ni2+ uptake by CorA
-
strictosamide
-
the main glycoalkaloid of Sarcocephalus latifolius leaves and roots, isolated from an ethanolic extract, used as medicinal plant in folk medicine, inhibits the enzyme in vitro and in vivo in kidney, but not in brain, by 45% at 2 mg/ml
tributyltin
-
TBT, one of the most toxic lipophilic aquatic pollutants. Maximal inhibition of 82% in the gills and 74% in the mantle at 0.00062 mM TBT, non-cooperative inhibition kinetics and a non-competitive mechanism with respect to ATP substrate, via formation of a TBT-Mg-ATPase complex, apparently more stable in the gills than in the mantle
Al3+
inhibits Alr1p and Alr2p; inhibits Alr1p and Alr2p
Ca2+
-
-
Ca2+
-
weak inhibition of CorA, MgtA, and MgtB
Co2+
-
-
Mg2+
the enzyme is highly sensitive to free magnesium in vitro and is strongly inhibited above 1 mM
Mn2+
-
short term exposure to Mn2+, at 50 mg/kg body weight, inhibits the enzyme by 9%, possibly due to Mg2+ replacement. The effect is increased by addition of cysteine
Mn2+
-
-
Mn2+
-
inhibition of CorA, MgtA, and MgtB, inhibition of CorA is noncompetitive, maximal 35% inhibition of MgtA at over 1 mM
Ni2+
-
-
additional information
-
the enzyme activity is not affected by (-)-epigallocatechine gallate
-
additional information
-
no inhibition of CorA by Fe2+ and Fe3+
-
additional information
-
no inhibition of Mg2+ or Ni2+ uptake by CorA through Fe2+
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cetyltrimethylammonium bromide
-
i.e. CTAB, Mg2+-ATPase activity of ECF1 is very resistant to inhibition by cetyltrimethylammonium bromide, lower concentrations of cetyltrimethylammonium bromide stimulate Mg2+-ATPase activity of ECF1
additional information
-
the enzyme activity is not affected by (-)-epigallocatechine gallate
-
additional information
-
low Mg2+ concentration, acidic media and the PhoP regulator induce mgtC expression in Salmonella enterica serovar Typhi
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.02 - 0.03
Co2+
-
pH 7.4, 37°C, CorA
0.01 - 0.015
Mg2+
-
pH 7.4, 37°C, CorA
additional information
additional information
-
Mg2+ uptake kinetics for CorA
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
inhibition kinetics, the inhibition by tributyltin follows a noncooperative kinetics in both tissues, gill and mantle
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.01 - 0.015
cetyltrimethylammonium bromide
Escherichia coli
-
pH 8.0, 37°C, inhibitory epsilon subunit, CF1-epsilon
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
determination of membrane potential of wild-type and transformed HEK-293 cell mitochondria, overview
additional information
Mg2+ transport measurements by patch clamp technique
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.2
7.4
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
periplasmic domain, expression in Escherichia coli
Swissprot
brenda
recombinant periplasmic domain, glutathione S-transferase fusion protein
-
-
brenda
serovar Typhi, a Chilean clinical isolate of the human specific pathogen
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Madin-Darby kidney cell, basolateral localization of both endogenous and ectopically expressed transporter CNNM4. Single knockdown of my1B, a cargo-recognition subunit of AP-1B, does not affect basolateral localization, but simultaneous knockdown of the my1A subunit of AP-1A abrogates localization
brenda
additional information
additional information
expression mainly in plant aerial tissues when Mg2+ levels are high in the soil or growth medium
brenda
additional information
-
constitutive expression of corA
brenda
additional information
-
nonrepressible constitutive expression of CorA
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
Mrs2 is the major transport protein for Mg2+ uptake into mitochondria
brenda
basolateral localization of both endogenous and ectopically expressed transporter CNNM4. Single knockdown of my1B, a cargo-recognition subunit of AP-1B, does not affect basolateral localization, but simultaneous knockdown of the my1A subunit of AP-1A abrogates localization
brenda
-
the CorA monomer has a C-terminal membrane domain containing two transmembrane segments
brenda
the transmembrane helices are connected by 5 loops, structure, overview
brenda
Mrs2p
brenda
Mrs2p contains two adjacent transmembrane domains near the C terminus of Mrs2p one of which ends with a F/Y-G-M-N motif
brenda
-
seasonal variations in Mg2+-ATPase activity of rat heart mitochondria
brenda
-
both N-terminus and C-terminus of Alr1p and Alr2p are exposed to the inner side of the plasma membrane
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
the enzyme acts as a sensor as well as a transporter of Mg2+
physiological function
physiological function
overexpression of MagT1 in Transient Receptor Potential Melastatin 7 (TRPM7)-deficient cells augments their capacity to uptake Mg2+, and improves their growth behavior in the absence of excess Mg2+
physiological function
-
the MgtA protein mediates Mg2+ uptake from the periplasm into the cytoplasm
physiological function
Q7CIZ1
inactivation of magnesium transporter MgtB leads to a reduced growth relative to the wild-type, even in media supplemented with 1 mM Mg2+. MgtB mutants survive equally as well as the respective parent strain within macrophages, although they are more sensitive to killing in the Galleria model of infection. MgtB is required for macrophage invasion in Yersinia pestis. Yersinia MgtB deletion mutants are more highly attenuated than the equivalent Yersinia PhoP two-component regulatory system deletion mutants in mouse models of infection
physiological function
-
inactivation of magnesium transporter MgtB leads to a reduced growth relative to the wild-type, even in media supplemented with 1 mM Mg2+. MgtB mutants survive equally as well as the respective parent strain within macrophages, although they are more sensitive to killing in the Galleria model of infection. Yersinia MgtB deletion mutants are more highly attenuated than the equivalent Yersinia PhoP two-component regulatory system deletion mutants in mouse models of infection
physiological function
-
mutants lacking transproter Alr1 activity show sensitivity to deprivation and excess Mg2+ and Ca2+. They also exhibit an autonomous ascospore maturation defect. Mutant ascospores are arrested at an early stage when they contain two nuclei
physiological function
-
overexpression of Bacillus subtilis MgtE is able to rescue the growth of DT40 B-cells lacking lacking the ion-channel kinase transient receptor potential cation channel, TRPM7. There is no detectable current development in TRPM7-deficient cells expressing MgtE. In DT40 B-cells, MgtE expression is strongly downregulated at high magnesium concentrations. The N-terminal cytoplasmic domain of MgtE is required for normal MgtE channel function
physiological function
silencing of MGT6 in transgenic plants by RNA interference results in growth retardation under the low-Mg2+ condition. RNAi plants contain lower levels of Mg2+ compared with wild-type plants under low Mg2+ but not under Mg2+-sufficient conditions. MGT6 plays a key role in Mg2+ uptake by roots under Mg2+ limitation
physiological function
-
magnesium transporter MgtE inhibits type III secretion system gene expression by stimulating rsmYZ transcription. The translation of the transcriptional activator ExsA is repressed by expression of the enzyme
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
102000
37000
39000
42000
55000
x * 55000, about, recombinant HA-tagged wild-type and mutant enzymes, SDS-PAGE
42000
5 * 42000, about, SDS-PAGE, a funnel-shaped homopentamer with two transmembrane helices per monomer, the large cytosolic domain forms the funnel, overview
42000
-
5 * 42000, about, SDS-PAGE, CorA is a homopentamer with two transmembrane domains per monomer, the first of which forms the ion conduction pathway, CorA structure analysis, overview
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oligomer
pentamer
tetramer
additional information
?
x * 55000, about, recombinant HA-tagged wild-type and mutant enzymes, SDS-PAGE
?
-
x * 55000, about, recombinant HA-tagged wild-type and mutant enzymes, SDS-PAGE
-
oligomer
Alr1p is at least a tetramer, Alr1p and Alr2p form homooligomers, but heteroligomers when overexpressed, the oligomerization of Alr1p results in a dominant negative action on the protein
oligomer
Alr2p forms homooligomers, but heteroligomers when overexpressed
pentamer
-
5 * 42000, about, SDS-PAGE, CorA is a homopentamer with two transmembrane domains per monomer, the first of which forms the ion conduction pathway, CorA structure analysis, overview
pentamer
5 * 42000, about, SDS-PAGE, a funnel-shaped homopentamer with two transmembrane helices per monomer, the large cytosolic domain forms the funnel, overview
pentamer
-
the CorA monomer has a C-terminal membrane domain containing two transmembrane segments, and a large, highly negatively charged N-terminal cytoplasmic soluble domain, the enzyme forms a homopentamer shaped like a funnel, which interacts with the ring of positive charges external to the ion conduction pathway at the cytosolic membrane interface, in the membrane
tetramer
-
cross-linking experiments with wild-type and mutants carrying additional Cys residues or lacking Cys residues
additional information
-
isoforms Alr1p and Alr2p form homo-oligomers as well as hetero-oligomers
additional information
two coiled-coil domains and several conserved primary sequences block in the central part of Mrs2p
additional information
-
two coiled-coil domains and several conserved primary sequences block in the central part of Mrs2p
additional information
CorA contains an unusually long ion pore putatively gated by hydrophobic residues near the intracellular end and by universally conserved asparagine residues at the periplasmic entrance
additional information
secondary structure determination and analysis
additional information
structural basis for Mg2+ homeostasis and the CorA translocation cycle, open state model and two-state model, overview
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
disulfide bonds do not participate in tetramer formation
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
single particle electron microscopy of recombinant periplasmic domain, enzyme is a pyramid-like homotetramer with a central cavity
-
both full-length enzyme and isolated cytoplasmic domain. Enzyme forms a funnel-shaped homopentamer with two transmembrane domains per monomer. An Mg2+ ion is bound between monomers at a conserved site in the cytoplasmic domain
-
crystal structure analysis from PDB ID BBJ2 at 3.9 A resolution for the whole enzyme, and at 1.8 A resolution for the soluble domain, overview
crystal structure analysis, X-ray structure determination at 3.9 A resolution, PDB ID 2BBJ, overview
-
enzyme forms a pentameric cone-shaped structure with regulatory metal binding sites in the N-terminal domain
-
free wild-type CorA, CorA1-351, and SeMet-AfCorA1-263, in complex with several different metal ions, 15 mg/ml purified CorA1-351 in 20 mM Tris pH 8.0, 100 mM NaCl, 1 mM TCEP, with or without 0.026% n-dodecyl-beta-D-maltoside, with precipitant vapor-diffusion over 20% PEG 400, 0.2 M CaCl2, 0.1 M HEPES, pH 7.0, 40 mg/ml native and SeMet-AfCorA1-263 from 1.3 M ammonium sulfate, 10 mM CoCl2, 0.1 M HEPES, pH 7.4, X-ray diffraction structure determination and analysis at 3.7 A resolution
recombinant enzyme, purification omits the isolation and subsequent solubilization of the membrane fraction
selenomethionine-labeled full-length enzyme and soluble cytosolic domain in presence and absence of Mg2+, 10 mg/ml full-length protein with 0.1% dodecylmaltoside, by vapour diffusion over 32-34% 2-methyl-2,4-pentanediol, 40 mM magnesium acetate, and 100 mM MES, pH 6.0, cytosolic domain with bound Mg2+ by vapour diffusion over solutions containing 18-22% PEG 400, 0.2M MgCl2, and 0.1M HEPES, pH 7.4, or cytosolic domain in the absence of Mg2+ in 20% PEG 3350, 0.2 M ammonium acetate, and 0.5% octyl-beta-D-glucopyranoside, X-ray diffraction structure determination at 2.3-3.9 A resolution, multiple anomaleous dispersion method
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C191A
-
elimination of the only Cys residue of enzyme, mutant forms a tetramer like wild-type
L323A/L324A
mutation in potential basolateral sorting signal, does not affect basolateral localization of isoform CNNM4
L550A/L551A/L552A
mutation in potential basolateral sorting signal, does not affect basolateral localization of isoform CNNM4
L575A/L576A
mutation in potential basolateral sorting signal, mutant protein is expressed on both apical and basolateral surfaces in approximately half of the observed cells
L575A/L576A/L758A/L759A/L765A/L766A
mutation in potential basolateral sorting signals, mutant protein is found on both apical and basolateral surfaces in almost all of the observed cells. Mutation disrupts interaction with my1A and my1B
L578A/L579A
mutation in potential basolateral sorting signal, mutant vprotein is observed throughout the cytoplasm
L758A/L759A
mutation in potential basolateral sorting signal, mutant protein is expressed on both apical and basolateral surfaces in approximately half of the observed cells
L765A/L766A
mutation in potential basolateral sorting signal, mutant protein is expressed on both apical and basolateral surfaces in approximately half of the observed cells
Y351A
mutation in potential basolateral sorting signal, does not affect basolateral localization of isoform CNNM4
Y405A
mutation in potential basolateral sorting signal, does not affect basolateral localization of isoform CNNM4
Y488A
mutation in potential basolateral sorting signal, does not affect basolateral localization of isoform CNNM4
Y581A
mutation in potential basolateral sorting signal, does not affect basolateral localization of isoform CNNM4
Y708A
mutation in potential basolateral sorting signal, mutant vprotein is observed throughout the cytoplasm
D235R
loss-of-function mutation, site-directed mutagenesis, growth phenotype, overview
D244K
loss-of-function mutation, site-directed mutagenesis, growth phenotype, overview
E341D
site-directed mutagenesis, the substitution in the loop region of Mrs2p does not influence conductance of the Mg2+ channel
E341K
site-directed mutagenesis, the substitution in the loop region of Mrs2p abolish conductance of the Mg2+ channel
E342D
site-directed mutagenesis, the substitution in the loop region of Mrs2p does not influence conductance of the Mg2+ channel
E342K
site-directed mutagenesis, the substitution in the loop region of Mrs2p abolish conductance of the Mg2+ channel
R173E
loss-of-function mutation, site-directed mutagenesis, growth phenotype, overview
R768E
-
isoform Alr2p, stimulation of Mg2+-transport activity of enzyme
E341D
-
site-directed mutagenesis, the substitution in the loop region of Mrs2p does not influence conductance of the Mg2+ channel
-
E341K
-
site-directed mutagenesis, the substitution in the loop region of Mrs2p abolish conductance of the Mg2+ channel
-
E342D
-
site-directed mutagenesis, the substitution in the loop region of Mrs2p does not influence conductance of the Mg2+ channel
-
E342K
-
site-directed mutagenesis, the substitution in the loop region of Mrs2p abolish conductance of the Mg2+ channel
-
C191S/C317
-
addition of a Cys residue to enzyme cytoplasmic C-terminus, mutant retains function
E281A
the mutant shows no significant changes in apparent Mg2+ affinity
E281K/K287E
the apparent cation affinity of the double mutant is identical to that of wild type enzyme
E281L
the mutant shows no significant changes in apparent Mg2+ affinity
E281Q
the mutant shows no significant changes in apparent Mg2+ affinity
E281R
the mutant shows no significant changes in apparent Mg2+ affinity
K287E
the mutation demonstrates a modest decrease in apparent Mg2+ affinity of 2-4fold, the mutation does not affect enzyme function significantly, although apparent Mg2+ affinity is decreased about 10fold
K287Q
the mutation does not affect enzyme function significantly, although apparent Mg2+ affinity is decreased about 10fold
K287R
the mutation does not affect enzyme function significantly, although apparent Mg2+ affinity is decreased about 10fold
P555A
-
the MgtB mutant is functional for transporting Mg2+ to support growth in low Mg2+ media and shows higher replication within macrophages compared to the wild type
P556A
-
the MgtB mutant is functional for transporting Mg2+ to support growth in low Mg2+ media and shows higher replication within macrophages compared to the wild type
Y292C
-
cross-linking in presence of Cu(II)-1,10-phenanthroline and spontaneously
P555A
-
the MgtB mutant is functional for transporting Mg2+ to support growth in low Mg2+ media and shows higher replication within macrophages compared to the wild type
-
P556A
-
the MgtB mutant is functional for transporting Mg2+ to support growth in low Mg2+ media and shows higher replication within macrophages compared to the wild type
-
M299A
-
mutant with decreased cation affinity
M299C
-
mutant with decreased cation affinity
Y292C
-
mutant with decreased transport properties
Y292F
-
mutant with decreased transport properties
Y292I
-
mutant with decreased transport properties
Y292S
-
mutant with decreased transport properties
Y307A
-
mutant with decreased cation affinity
Y307F
-
mutant with decreased cation affinity
Y307S
-
mutant with decreased cation affinity
D253F
site-directed mutagenesis, structural alterations and Mg2+ transport in comparison to the wild-type enzyme, overview
D253K
site-directed mutagenesis, structural alterations and Mg2+ transport in comparison to the wild-type enzyme, overview
D253W
site-directed mutagenesis, structural alterations and Mg2+ transport in comparison to the wild-type enzyme, overview
E206R
site-directed mutagenesis, structural alterations and Mg2+ transport in comparison to the wild-type enzyme, overview
E316K
site-directed mutagenesis, structural alterations and Mg2+ transport in comparison to the wild-type enzyme, overview
E316K/E320A
site-directed mutagenesis, with mutation of Gly4alpha5alpha6, structural alterations and Mg2+ transport in comparison to the wild-type enzyme, overview
E320K
site-directed mutagenesis, structural alterations and Mg2+ transport in comparison to the wild-type enzyme, overview
P303I
site-directed mutagenesis, structural alterations and Mg2+ transport in comparison to the wild-type enzyme, overview
V194E
site-directed mutagenesis, structural alterations and Mg2+ transport in comparison to the wild-type enzyme, overview
V194E/E206R
site-directed mutagenesis, structural alterations and Mg2+ transport in comparison to the wild-type enzyme, overview
additional information
additional information
-
mutant atmrs2-2 lacks any domain sufficiently hydrophobic to insert in a membrane and does not complement the yeast mutant, as does sibling atmrs2-1
additional information
-
functional complementation of Salmonella mutant strain MM281 by MGT9, disruption of MGT9 leads to abortion of half of the mature pollen grains in a heterozygous mutant and MGT9 RNAi transgenic plants, the homogenous mutation is lethal
additional information
-
enzyme knockout mutant causes hypersensitivity to the lactoperoxidase system. Repression of the Mg2+ stimulon by Mg2+ does not change the lactoperoxidase sensitivity of either wild-type or mutant. Prior exposure to Ni2+, which is also transported by the enzyme, strongly sensitizes wild-type, but not the mutant. Ni2+-dependent sensitzation is suppressed by the enzyme-specific inhibior Co(III)hexaammine
additional information
-
purified recombinant periplasmic domain of enzyme retains its substrate binding ability as native enzyme
additional information
-
selection of Mg2+ transport defect corA mutants by screening for Co2+ resistant strains, since accumulation of Co2+ is tosic for the cells
additional information
-
Mg2+-ATPase activities of CF1 deficient in its inhibitory epsilon subunit, CF1-epsilon, are sensitive to inhibition by melittin and by cetyltrimethylammonium bromide. Sulfite-activated Mg2+-ATPase activity of CF1-epsilon is inhibited by cetyltrimethylammonium bromide
additional information
-
conditional knock-down of MRS2 by stable long-term expression of specific shRNA in HEK-293 cells results in loss of mitochondrial Mg2+ uptake and cell death, overview
additional information
Alr1p mutants show 25-30% reduced Mg2+ content but fail to accumulate Mg2+
additional information
Alr1p mutants show 25-30% reduced Mg2+ content but fail to accumulate Mg2+
additional information
Alr1p mutants show 25-30% reduced Mg2+ content but fail to accumulate Mg2+
additional information
construction of the the isogenic mrs2D deletion strain DBY mrs2-1, and the mrs2D/lpe10D double disruptant DBY747 mrs2-2, lpe10-2, Mrs2p coiled-coil mutations results in elevated Mg21 influx into mitochondria
additional information
gain-of-function mutations, obtained upon random mutagenesis, map to the conserved primary sequences blocking in the central part of Mrs2, while site-directed mutations in several conserved sequences reduce Mrs2p-mediated Mg2+ uptake and decrease group II intron splicing both resulting in reduced steady-state Mg2+ concentrations, overview
additional information
-
gain-of-function mutations, obtained upon random mutagenesis, map to the conserved primary sequences blocking in the central part of Mrs2, while site-directed mutations in several conserved sequences reduce Mrs2p-mediated Mg2+ uptake and decrease group II intron splicing both resulting in reduced steady-state Mg2+ concentrations, overview
additional information
the mgtAmgtCB mutant strain is dependent on CorA for Mg2+ uptake and is completely growth-inhibited by cation hexaamines, Mrs2p mutants can be complemented by bacterial CorA, mrs2 mutants decreases Mg2+ uptake and Mg2+ content in the mitochondria by 62%
additional information
the mgtAmgtCB mutant strain is dependent on CorA for Mg2+ uptake and is completely growth-inhibited by cation hexaamines, Mrs2p mutants can be complemented by bacterial CorA, mrs2 mutants decreases Mg2+ uptake and Mg2+ content in the mitochondria by 62%
additional information
the mgtAmgtCB mutant strain is dependent on CorA for Mg2+ uptake and is completely growth-inhibited by cation hexaamines, Mrs2p mutants can be complemented by bacterial CorA, mrs2 mutants decreases Mg2+ uptake and Mg2+ content in the mitochondria by 62%
additional information
-
construction of the the isogenic mrs2D deletion strain DBY mrs2-1, and the mrs2D/lpe10D double disruptant DBY747 mrs2-2, lpe10-2, Mrs2p coiled-coil mutations results in elevated Mg21 influx into mitochondria
-
additional information
-
enzyme knockout mutant causes hypersensitivity to the lactoperoxidase system. Repression of the Mg2+ stimulon by Mg2+ does not change the lactoperoxidase sensitivity of either wild-type or mutant. Prior exposure to Ni2+, which is also transported by the enzyme, strongly sensitizes wild-type, but not the mutant. Ni2+-dependent sensitzation is suppressed by the enzyme-specific inhibior Co(III)hexaammine
additional information
-
mutations of mgtA, mgtB, and corA result in protein incapable of Mg2+ ransport, the Mg2+ transport mutant MM281 can be rescued by complementation with corA from Bacillus firmus strain OB4 or Providencia stuartii, mutation of corA leads to attenuation of virulence and to other defects, but not to growth defects, the CorA-mediated Ni2+ uptake is 2fold increased in a phoP strain compared to wild-type without any increase in the amount of CorA protein
additional information
deletion mutant Gly4alpha5alpha6, site-directed mutagenesis, structural alterations and Mg2+ transport in comparison to the wild-type enzyme, overview
additional information
mutation of residues near L294/M291 alters the transport properties of CorA
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
Mutants defective in phoP or in both mgtA and mgtB are hypersensitive to oxidative stress-dependent Fe(II)-mediated killing
-
656828
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme, purification omits the isolation and subsequent solubilization of the membrane fraction
recombinant HA-tagged wild-type and mutant enzymes in yeast, native enzyme partially by preparation of mitochondria
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 by nickel affinity chromatography, cleavage of the His-tag, and gel filtration to homogeneity
recombinant N-terminally His-tagged cytosolic domain by nickel affinity chromatography, tag cleavage by thrombin, anion exchange chromatography and gel filtration, recombinant N-terminally His-tagged full-length MgtE from Escherichia coli strain C41 (DE3) by nickel affinity chromatography and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
CorA, MgtA, and MgtB
-
expression in Escherichia coli
-
expression of HA-tagged wild-type and mutant enzymes in yeast
expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21, complementation of Salmonella typhimurium MM281, a strain devoid of all genomic Mg2+ transport systems
expression of wild-type and mutant enzyme, the arginine rich motif of Mrs2p is not essential for the splicing of group II introns
gene corA, DNA and amino acid asequence determination
gene mgtE, expression in and functional complementation of a CorA Mg2+ transport mutant of Salmonella enterica serovar Thyphimurium
gene mgtE, overexpression of N-terminally His-tagged full-length enzyme and cytosolic domain in Escherichia coli strain C41 (DE3)
genes mgtA and mgtB, from complementation of the Mg2+ growth phenotype mutants MM7 and MM281, gene corA, DNA and amino acid sequence determination, the corA promoter does not respond to extracellular Mg2+ concentration, transcription factor PhoP is important in corA transcription regulation, overview
-
gene mgtE, expression in and functional complementation of a CorA Mg2+ transport mutant of Salmonella enterica serovar Thyphimurium
-
gene mgtE, expression in and functional complementation of a CorA Mg2+ transport mutant of Salmonella enterica serovar Thyphimurium
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression is highly induced in the roots during Mg2+ deficiency´
gene expression of the Mg2+ selective transporter MagT1 is upregulated in TRPM7-deficient cells. The enzyme level is elevated when cells are cultured in Mg2+ free medium for 24 h
in the unlesioned striatum, the levels of enzyme mRNA show an increasing trend after treatment with MgSO4 for 14 days
-
inactivation of elongation factor P derepresses transcription of the mgtCBR operon and decreases MgtB protein levels
mRNA and protein expressions in the lesioned striatum are lower in the 6-hydroxydopamine-lesioned rats than in the controls at both 7 and 14 days post-lesion induction
-
overexpression of the Mg2+ transporter CorA decreases mgtA transcription
-
Salmonella expresses the MgtA transporter only in Mg2+-depleted conditions. MgtA expression increases in a Salmonella strain lacking MgtR. The MgtR peptide is necessary for the MgtA protein to be induced at the normal timing upon Mg2+ starvation
the MgtR peptide limits levels of the MgtA protein at low Mg2+ concentrations
there is little mgtA transcription when strain YS802 is grown in media with more than 0.05 mM Mg2+, some transcription in 0.05 mM Mg2+, and maximum levels in 0.01 mM Mg2+
-
inactivation of elongation factor P derepresses transcription of the mgtCBR operon and decreases MgtB protein levels
-
inactivation of elongation factor P derepresses transcription of the mgtCBR operon and decreases MgtB protein levels
-
-
Salmonella expresses the MgtA transporter only in Mg2+-depleted conditions. MgtA expression increases in a Salmonella strain lacking MgtR. The MgtR peptide is necessary for the MgtA protein to be induced at the normal timing upon Mg2+ starvation
Salmonella expresses the MgtA transporter only in Mg2+-depleted conditions. MgtA expression increases in a Salmonella strain lacking MgtR. The MgtR peptide is necessary for the MgtA protein to be induced at the normal timing upon Mg2+ starvation
-
-
the MgtR peptide limits levels of the MgtA protein at low Mg2+ concentrations
the MgtR peptide limits levels of the MgtA protein at low Mg2+ concentrations
-
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
reconstitution of the purified recombinant enzyme in phosphatidylcholine liposomes, overview
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
-
Overexpression of enzyme in Escherichia coli results in formation of inclusion bodies. Co-expression of DnaK/DnaJ prevents inclusion bodies and leads to the integration of more enzyme into the membrane. Co-expression of GroEL/GroES, Ffh/4.5S-RNA or SecA are less effective
medicine
synthesis
by overexpression of mgtA in Escherichia coli, a concentration of 32.41 g succinic acid per liter with a yield of 0.81 g per g glucose, can be obtained in a batch fermentation by using the low-cost mixture of Mg(OH)2 and NH3-H2O to replace MgCO3 as the alkaline neutralizer. The effect of the inhibitory compounds in lignocellulosic hydrolyzates on cell growth and succinic acid production can be relieved. In a 3-liter bioreactor, the overall productivity and yield of succinic acid in the whole anaerobic stage are 2.15 g per liter and h and 0.86 g per g total sugar, respectively
medicine
-
Mg2+ transport
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Snavely, M.D.; Florer, J.B.; Miller, C.G.; Maguire, M.E.
Magnesium transport in Salmonella typhimurium: Expression of cloned genes for three distinct Mg2+ transport systems
J. Bacteriol.
171
4752-4760
1988
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Snavely, M.D.; Florer, J.B.; Miller, C.G.; Maguire, M.E.
Magnesium transport in Salmonella typhimurium: 28Mg2+ transport by the CorA, MgtA, and MgtB systems
J. Bacteriol.
171
4761-4766
1989
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Snavely, M.D.; Miller, C.G.; Maguire, M.E.
The mgtB Mg2+ transport locus of Salmonella typhimurium encodes a P-type ATPase
J. Biol. Chem.
266
815-823
1991
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Snavely, M.D.; Gravina, S.A.; Cheung, T.T.; Miller, C.G.
Magnesium transport in Salmonella typhimurium
J. Biol. Chem.
266
824-829
1991
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Taffet, G.E.; Tate, C.A.
The MgATPase activity of rat cardiac sarcoplasmic reticulum is a function of the calcium ATPase protein
Arch. Biochem. Biophys.
299
287-294
1992
Rattus norvegicus
brenda
Maguire, M.E.; Snavely, M.D.; Leizman, J.B.; Gura, S.; Bagga, D.; Tao, T.; Smith, D.L.
Mg2+ transporting P-type ATPases of Salmonella typhimurium
Ann. N. Y. Acad. Sci.
671
244-255
1992
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Maguire, M.E.
MgtA and MgtB: Prokaryotic P-type ATPases that mediate Mg2+ influx
J. Bioenerg. Biomembr.
24
319-328
1992
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Smith, D.L.; Tao, T.; Maguire, M.E.
Membrane topology of a P-type ATPase. The MgtB magnesium transport protein of Salmonella typhimurium
J. Biol. Chem.
268
22469-22479
1993
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Smith, R.L.; Banks, J.L.; Snavely, M.D.; Maguire, M.E.
Sequence and topology of the CorA magnesium transport systems of Salmonella typhimurium and Escherichia coli
J. Biol. Chem.
268
14071-14080
1993
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Tao, T.; Snavely, M.D.; Farr, S.G.; Maguire, M.E.
Magnesium transport in Salmonella typhimurium: mgtA encodes a P-type ATPase and is regulated by Mg2+ in a manner similar to that of the mgtB P-type ATPase
J. Bacteriol.
177
2654-2662
1995
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Smith, R.L.; Maguire, M.E.
Distribution of the CorA Mg2+ transport system in gram-negative bacteria
J. Bacteriol.
177
1638-1640
1995
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Smith, R.L.; Szegedy, M.A.; Kucharski, L.M.; Walker, C.; Wiet, R.M.; Redpath, A.; Kaczmarek, M.T.; Maguire, M.E.
The CorA Mg2+ transport protein of Salmonella typhimurium. Mutagenesis of conserved residues in the third membrane domain identifies a Mg2+ pore
J. Biol. Chem.
273
28663-28669
1998
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Tao, T.; Grulich, P.F.; Kucharski, L.M.; Smith, R.L.; Maguire, M.E.
Magnesium transport in Salmonella typhimurium: biphasic magnesium and time dependence of the transcription of the mgtA and mgtCB loci
Microbiology
144
655-664
1998
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Smith, R.L.; Kaczmarek, M.T.; Kucharski, L.M.; Maguire, M.E.
Magnesium transport in Salmonella typhimurium: regulation of mgtA and mgtCB during invasion of epithelial and macrophage cells
Microbiology
144
1835-1843
1998
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Moncrief, M.B.C.; Maguire, M.E.
Magnesium and the role of mgtC in growth of Salmonella typhimurium
Infect. Immun.
66
3802-3809
1998
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Smith, R.L.; Gottlieb, E.; Kucharski, L.M.; Maguire, M.E.
Functional similarity between archaeal and bacterial CorA magnesium transporters
J. Bacteriol.
180
2788-2791
1998
Methanocaldococcus jannaschii, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Smith, R.L.; Maguire, M.E.
Microbial magnesium transport: unusual transporters searching for identity
Mol. Microbiol.
28
217-226
1998
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Kucharski, L.M.; Lubbe, W.J.; Maguire, M.E.
Cation hexaammines are selective and potent inhibitors of the CorA magnesium transport system
J. Biol. Chem.
275
16767-16773
2000
Methanocaldococcus jannaschii, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Kehres, D.G.; Maguire M.E.
Structure, properties and regulation of magnesium transport proteins
Biometals
15
261-270
2002
Salmonella enterica
brenda
Chamnongpol, S.; Groisman, E.A.
Mg2+ homeostasis and avoidance of metal toxicity
Mol. Microbiol.
44
561-571
2002
Salmonella enterica
brenda
Li, L.; Tutone, A.F.; Drummond R.S.M.; Gardner R.C.; Luan S.
A novel family of magnesium transport genes in Arabidopsis
Plant Cell
13
2761-2775
2001
Arabidopsis sp.
brenda
Payandeh, J.; Pai, E.F.
Crystallization and preliminary X-ray diffraction analysis of the magnesium transporter CorA
Acta Crystallogr. Sect. F
62
148-152
2006
Archaeoglobus fulgidus (O29487), Archaeoglobus fulgidus, Thermotoga maritima (Q9WZ31), Thermotoga maritima
brenda
Sermon, J.; Wevers, E.M.; Jansen, L.; De Spiegeleer, P.; Vanoirbeek, K.; Aertsen, A.; Michiels, C.W.
CorA affects tolerance of Escherichia coli and Salmonella enterica serovar Typhimurium to the lactoperoxidase enzyme system but not to other forms of oxidative stress
Appl. Environ. Microbiol.
71
6515-6523
2005
Escherichia coli, Salmonella enterica
brenda
Wachek, M.; Aichinger, M.C.; Stadler, J.A.; Schweyen, R.J.; Graschopf, A.
Oligomerization of the Mg2+-transport proteins Alr1p and Alr2p in yeast plasma membrane
FEBS J.
273
4236-4249
2006
Saccharomyces cerevisiae
brenda
Warren, M.A.; Kucharski, L.M.; Veenstra, A.; Shi, L.; Grulich, P.F.; Maguire, M.E.
The CorA Mg2+ transporter is a homotetramer
J. Bacteriol.
186
4605-4612
2004
Bacillus subtilis, Salmonella enterica, Methanocaldococcus jannaschii
brenda
Papp, K.M.; Maguire, M.E.
The CorA Mg2+ transporter does not transport Fe2+
J. Bacteriol.
186
7653-7658
2004
Salmonella enterica
brenda
Wang, S.Z.; Chen, Y.; Sun, Z.H.; Zhou, Q.; Sui, S.F.
Escherichia coli CorA periplasmic domain functions as a homotetramer to bind substrate
J. Biol. Chem.
281
26813-26820
2006
Escherichia coli
brenda
Lunin, V.V.; Dobrovetsky, E.; Khutoreskaya, G.; Zhang, R.; Joachimiak, A.; Doyle, D.A.; Bochkarev, A.; Maguire, M.E.; Edwards, A.M.; Koth, C.M.
Crystal structure of the CorA Mg2+ transporter
Nature
440
833-837
2006
Thermotoga maritima
brenda
Chen, Y.; Song, J.; Sui, S.F.; Wang, D.N.
DnaK and DnaJ facilitated the folding process and reduced inclusion body formation of magnesium transporter CorA overexpressed in Escherichia coli
Protein Expr. Purif.
32
221-231
2003
Escherichia coli
brenda
Eshaghi, S.; Niegowski, D.; Kohl, A.; Martinez Molina, D.; Lesley, S.A.; Nordlund, P.
Crystal structure of a divalent metal ion transporter CorA at 2.9 Angstrom resolution
Science
313
354-357
2006
Thermotoga maritima
brenda
Schindl, R.; Weghuber, J.; Romanin, C.; Schweyen, R.J.
Mrs2p forms a high conductance Mg2+ selective channel in mitochondria
Biophys. J.
93
3872-3883
2007
Saccharomyces cerevisiae (Q02783), Saccharomyces cerevisiae DBY747 (Q02783)
brenda
Maguire, M.E.
The structure of CorA: a Mg(2+)-selective channel
Curr. Opin. Struct. Biol.
16
432-438
2006
Thermotoga maritima
brenda
Payandeh, J.; Pai, E.F.
A structural basis for Mg2+ homeostasis and the CorA translocation cycle
EMBO J.
25
3762-3773
2006
Thermotoga maritima (Q9WZ31)
brenda
Weghuber, J.;Dieterich, F.; Froschauer, E.M.; Svidova, S.; Schweyen, R.J.
Mutational analysis of functional domains in Mrs2p, the mitochondrial Mg2+ channel protein of Saccharomyces cerevisiae
FEBS J.
273
1198-1209
2006
Saccharomyces cerevisiae (Q02783), Saccharomyces cerevisiae
brenda
Maguire, M.E.
Magnesium transporters: properties, regulation and structure
Front. Biosci.
11
3149-3163
2006
Aeromonas hydrophila, Arabidopsis thaliana, Cytobacillus firmus, Escherichia coli, Methanosarcina sp., Mycobacterium tuberculosis, Providencia stuartii, Salmonella enterica subsp. enterica serovar Typhimurium, Methanothermobacter sp., Methanocaldococcus jannaschii (Q58439), Thermotoga maritima (Q9WZ31), Cytobacillus firmus OF4
brenda
Payandeh, J.; Li, C.; Ramjeesingh, M.; Poduch, E.; Bear, C.E.; Pai, E.F.
Probing structure-function relationships and gating mechanisms in the CorA Mg2+ transport system
J. Biol. Chem.
283
11721-11733
2008
Thermotoga maritima (Q9WZ31)
brenda
Tripathi, V.N.; Srivastava, S.
Ni2+-uptake in Pseudomonas putida strain S4: a possible role of Mg2+-uptake pump
J. Biosci.
31
61-67
2006
Pseudomonas putida, Pseudomonas putida s4
brenda
Papp-Wallace, K.M.; Maguire, M.E.
Bacterial homologs of eukaryotic membrane proteins: the 2-TM-GxN family of Mg2+ transporters (Review)
Mol. Membr. Biol.
24
351-356
2007
Escherichia coli, Saccharomyces cerevisiae (P43553), Saccharomyces cerevisiae (Q02783), Saccharomyces cerevisiae (Q08269), Salmonella enterica subsp. enterica serovar Typhimurium, Thermotoga maritima (Q9WZ31)
brenda
Hattori, M.; Tanaka, Y.; Fukai, S.; Ishitani, R.; Nureki, O.
Crystal structure of the MgtE Mg2+ transporter
Nature
448
1072-1075
2007
Thermus thermophilus (Q5SMG8), Thermus thermophilus
brenda
Liapi, C.; Zarros, A.; Galanopoulou, P.; Theocharis, S.; Skandali, N.; Al-Humadi, H.; Anifantaki, F.; Gkrouzman, E.; Mellios, Z.; Tsakiris, S.
Effects of short-term exposure to manganese on the adult rat brain antioxidant status and the activities of acetylcholinesterase, (Na,K)-ATPase and Mg-ATPase: modulation by L-cysteine
Basic Clin. Pharmacol. Toxicol.
103
171-175
2008
Rattus norvegicus
brenda
Datiles, M.J.; Johnson, E.A.; McCarty, R.E.
Inhibition of the ATPase activity of the catalytic portion of ATP synthases by cationic amphiphiles
Biochim. Biophys. Acta
1777
362-368
2008
Escherichia coli
brenda
Liapi, C.; Zarros, A.; Theocharis, S.; Al-Humadi, H.; Anifantaki, F.; Gkrouzman, E.; Mellios, Z.; Skandali, N.; Tsakiris, S.
The neuroprotective role of L-cysteine towards the effects of short-term exposure to lanthanum on the adult rat brain antioxidant status and the activities of acetylcholinesterase, (Na+,K+)- and Mg2+-ATPase
Biometals
22
329-335
2009
Rattus norvegicus
brenda
Chen, J.; Li, L.G.; Liu, Z.H.; Yuan, Y.J.; Guo, L.L.; Mao, D.D.; Tian, L.F.; Chen, L.B.; Luan, S.; Li, D.P.
Magnesium transporter AtMGT9 is essential for pollen development in Arabidopsis
Cell Res.
19
887-898
2009
Arabidopsis thaliana
brenda
Liapi, C.; Kyriakaki, A.; Zarros, A.; Al-Humadi, H.; Stolakis, V.; Gkrouzman, E.; Anifantaki, F.; Skandali, N.; Margaritis, M.; Tsakiris, S.
Effects of adult-onset choline deprivation on the activities of acetylcholinesterase, (Na+,K+)- and Mg2+-ATPase in crucial rat brain regions
Food Chem. Toxicol.
47
82-85
2009
Rattus norvegicus
brenda
Piskacek, M.; Zotova, L.; Zsurka, G.; Schweyen, R.J.
Conditional knock-down of hMRS2 results in loss of mitochondrial Mg2+ uptake and cell death
J. Cell. Mol. Med.
13
693-700
2009
Homo sapiens
brenda
Candeias, M.F.; Abreu, P.; Pereira, A.; Cruz-Morais, J.
Effects of strictosamide on mouse brain and kidney Na+, K+-ATPase and Mg2+-ATPase activities
J. Ethnopharmacol.
121
117-122
2009
Mus musculus
brenda
Devika, P.T.; Mainzen Prince, P.S.
(-)-Epigallocatechin gallate (EGCG) prevents isoprenaline-induced cardiac marker enzymes and membrane-bound ATPases
J. Pharm. Pharmacol.
60
125-133
2008
Rattus norvegicus
brenda
Mujkosova, J.; Ferko, M.; Humenik, P.; Waczulikova, I.; Ziegelhoffer, A.
Seasonal variations in properties of healthy and diabetic rat heart mitochondria: Mg2+-ATPase activity, content of conjugated dienes and membrane fluidity
Physiol. Res.
57 Suppl 2
S75-S82
2008
Rattus norvegicus
brenda
Retamal, P.; Castillo-Ruiz, M.; Mora, G.C.
Characterization of MgtC, a virulence factor of Salmonella enterica Serovar Typhi
PLoS ONE
4
e5551
2009
Salmonella enterica
brenda
Pagliarani, A.; Bandiera, P.; Ventrella, V.; Trombetti, F.; Pirini, M.; Nesci, S.; Borgatti, A.R.
Tributyltin (TBT) inhibition of oligomycin-sensitive Mg-ATPase activity in mussel mitochondria
Toxicol. in Vitro
22
827-836
2008
Mytilus galloprovincialis
brenda
Choi, E.; Lee, K.Y.; Shin, D.
The MgtR regulatory peptide negatively controls expression of the MgtA Mg2+ transporter in Salmonella enterica serovar Typhimurium
Biochem. Biophys. Res. Commun.
417
318-323
2012
Salmonella enterica (D0ZTB2), Salmonella enterica 14028s (D0ZTB2)
brenda
Moomaw, A.S.; Maguire, M.E.
Cation selectivity by the CorA Mg2+ channel requires a fully hydrated cation
Biochemistry
49
5998-6008
2010
Salmonella enterica (P0A2R8)
brenda
Sponder, G.; Svidova, S.; Schindl, R.; Wieser, S.; Schweyen, R.J.; Romanin, C.; Froschauer, E.M.; Weghuber, J.
Lpe10p modulates the activity of the Mrs2p-based yeast mitochondrial Mg2+ channel
FEBS J.
277
3514-3525
2010
Saccharomyces cerevisiae, Saccharomyces cerevisiae DBY747
brenda
Deason-Towne, F.; Perraud, A.L.; Schmitz, C.
The Mg2+ transporter MagT1 partially rescues cell growth and Mg2+ uptake in cells lacking the channel-kinase TRPM7
FEBS Lett.
585
2275-2278
2011
Gallus gallus (Q5ZJ06)
brenda
Cromie, M.; Groisman, E.
Promoter and riboswitch control of the Mg2+ transporter MgtA from Salmonella enterica
J. Bacteriol.
192
604-607
2010
Salmonella enterica, Salmonella enterica YS802
brenda
de Azeredo-Oliveira, M.T.; da Silva, T.L.; Mello, M.L.
Mg2+-dependent ATPase activity in Malpighian tubules of Triatoma infestans Klug
Micron
43
298-304
2012
Triatoma infestans
brenda
Hirata, Y.; Funato, Y.; Miki, H.
Basolateral sorting of the Mg2+ transporter CNNM4 requires interaction with AP-1A and AP-1B
Biochem. Biophys. Res. Commun.
455
184-189
2014
Homo sapiens (Q6P4Q7)
brenda
Wang, J.; Zhang, B.; Zhang, J.; Wang, H.; Zhao, M.; Wang, N.; Dong, L.; Zhou, X.; Wang, D.
Enhanced succinic acid production and magnesium utilization by overexpression of magnesium transporter mgtA in Escherichia coli mutant
Biores. Technol.
170
125-131
2014
Escherichia coli (P0ABB8), Escherichia coli
brenda
Grognet, P.; Lalucque, H.; Silar, P.
The PaAlr1 magnesium transporter is required for ascospore development in Podospora anserina
Fungal Biol.
116
1111-1118
2012
Podospora anserina
brenda
Ford, D.C.; Joshua, G.W.; Wren, B.W.; Oyston, P.C.
The importance of the magnesium transporter MgtB for virulence of Yersinia pseudotuberculosis and Yersinia pestis
Microbiology
160
2710-2717
2014
Yersinia pseudotuberculosis, Yersinia pestis (Q7CIZ1), Yersinia pestis
brenda
Mao, D.; Chen, J.; Tian, L.; Liu, Z.; Yang, L.; Tang, R.; Li, J.; Lu, C.; Yang, Y.; Shi, J.; Chen, L.; Li, D.; Luan, S.
Arabidopsis transporter MGT6 mediates magnesium uptake and is required for growth under magnesium limitation
Plant Cell
26
2234-2248
2014
Arabidopsis thaliana (Q93ZD7)
brenda
Sahni, J.; Song, Y.; Scharenberg, A.M.
The B. subtilis MgtE magnesium transporter can functionally compensate TRPM7-deficiency in vertebrate B-cells
PLoS ONE
7
e44452
2012
Bacillus subtilis
brenda
Lin, L.; Yan, M.; Wu, B.; Lin, R.; Zheng, Z.
Expression of magnesium transporter SLC41A1 in the striatum of 6-hydroxydopamine-induced parkinsonian rats
Brain Res. Bull.
142
338-343
2018
Rattus norvegicus
brenda
Subramani, S.; Perdreau-Dahl, H.; Morth, J.P.
The magnesium transporter A is activated by cardiolipin and is highly sensitive to free magnesium in vitro
eLife
5
e11407
2016
Escherichia coli (P0ABB8), Escherichia coli
brenda
Anhe, A.; Azeredo-Oliveira, M.
Mg2+-dependent ATPase activity in triatomine salivary glands (Heteroptera, Triatominae)
Iheringia Ser. Zool.
107
e2017031
2017
Triatoma infestans, Panstrongylus megistus
-
brenda
Chakravarty, S.; Melton, C.N.; Bailin, A.; Yahr, T.L.; Anderson, G.G.
Pseudomonas aeruginosa magnesium transporter MgtE inhibits type III secretion system gene expression by stimulating rsmYZ transcription
J. Bacteriol.
199
e00268
2017
Pseudomonas aeruginosa
brenda
Choi, E.; Choi, S.; Nam, D.; Park, S.; Han, Y.; Lee, J.S.; Lee, E.J.
Elongation factor P restricts Salmonellas growth by controlling translation of a Mg2+ transporter gene during infection
Sci. Rep.
7
42098
2017
Salmonella enterica, Salmonella enterica 14028s
brenda
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