Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + H2O + Mg2+[side 1] = ADP + phosphate + Mg2+[side 2]
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
-
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
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + H2O + Co2+/in
ADP + phosphate + Co2+/out
-
apparent dissociation constant: wild-type, 0.0298 mM, recombinant periplasmic domain, 0.0236 mM
-
-
?
ATP + H2O + Co2+/out
ADP + phosphate + Co2+/in
ATP + H2O + Mg2+/in
ADP + phosphate + Mg2+/out
-
apparent dissociation constant: wild-type, 0.0184 mM, recombinant periplasmic domain, 0.0309 mM9
-
-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
ATP + H2O + Mg2+[side 1]
ADP + phosphate + Mg2+[side 2]
ATP + H2O + Ni2+/in
ADP + phosphate + Ni2+/out
ATP + H2O + Ni2+/out
ADP + phosphate + Ni2+/in
additional information
?
-
ATP + H2O + Co2+/out
ADP + phosphate + Co2+/in
-
-
-
-
?
ATP + H2O + Co2+/out
ADP + phosphate + Co2+/in
-
-
-
-
?
ATP + H2O + Co2+/out
ADP + phosphate + Co2+/in
-
-
-
-
?
ATP + H2O + Co2+/out
ADP + phosphate + Co2+/in
-
-
-
?
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
-
-
-
-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
-
-
-
-
?
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
-
-
-
-
?
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
-
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
-
-
-
?
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
-
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
-
-
-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
-
-
-
-
?
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
-
-
-
-
?
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
-
-
?
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
-
-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
-
-
-
-
?
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
-
-
-
-
?
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
-
-
?
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
-
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
ATP + H2O + Mg2+[side 1]
ADP + phosphate + Mg2+[side 2]
-
-
-
?
ATP + H2O + Mg2+[side 1]
ADP + phosphate + Mg2+[side 2]
-
-
-
-
?
ATP + H2O + Mg2+[side 1]
ADP + phosphate + Mg2+[side 2]
-
-
-
-
?
ATP + H2O + Mg2+[side 1]
ADP + phosphate + Mg2+[side 2]
-
-
-
-
?
ATP + H2O + Mg2+[side 1]
ADP + phosphate + Mg2+[side 2]
-
-
-
-
?
ATP + H2O + Mg2+[side 1]
ADP + phosphate + Mg2+[side 2]
-
-
-
-
?
ATP + H2O + Mg2+[side 1]
ADP + phosphate + Mg2+[side 2]
-
-
-
-
?
ATP + H2O + Ni2+/in
ADP + phosphate + Ni2+/out
-
apparent dissociation constant: wild-type, 0.201 mM, recombinant periplasmic domain, 0.106 mM
-
-
?
ATP + H2O + Ni2+/in
ADP + phosphate + Ni2+/out
-
-
-
-
?
ATP + H2O + Ni2+/out
ADP + phosphate + Ni2+/in
-
-
-
-
?
ATP + H2O + Ni2+/out
ADP + phosphate + Ni2+/in
-
-
-
?
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
-
-
-
-
?
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
-
-
?
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
?
-
-
no substrate for transport: Fe2+
-
-
?
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
M1301
gain-of-function mutation, random mutagenesis
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
-
mutant retains function
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
E285A
non-functional mutant
E285D
non-functional mutant
E285K
non-functional mutant
E285Q
non-functional mutant
E285R
non-functional mutant
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
M299C
-
cross-linking in presence of Cu(II)-1,10-phenanthroline
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
S274C
-
cross-linking in presence of Cu(II)-1,10-phenanthroline
T270C
-
cross-linking in presence of Cu(II)-1,10-phenanthroline
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
-
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
-
enzyme knockout mutant, study on uptake of Fe2+
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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