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Information on EC 1.8.5.9 - protein dithiol:quinone oxidoreductase DsbB
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EC Tree
1.8.5.9 protein dithiol:quinone oxidoreductase DsbBIUBMB Comments
DsbB is a protein found in Gram-negative bacteria that functions within a pathway for protein disulfide bond formation. The enzyme catalyses the oxidation of the DsbA protein by generating disulfide bonds de novo via the reduction of membrane quinones. cf. EC 1.8.4.15, protein dithiol oxidoreductase (disulfide-forming).
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The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
=
+
a [DsbA protein] with reduced L-cysteine residues
+
=
a [DsbA protein] carrying a disulfide bond
+
Synonyms
ctdsbb, vkor homolog, disulfide bond formation protein b, disulfide bond protein b, disulfide-bond formation protein b, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C. trachomatis disulfide bond protein B
CtDsbB
disulfide bond oxidoreductase B
DsbB
membrane protein disulfide bond protein B
Rv2968c
VKOR homolog
DsbB
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a [DsbA protein] with reduced L-cysteine residues + a quinone = a [DsbA protein] carrying a disulfide bond + a quinol
overall reaction
-
-
-
a [DsbA protein] with reduced L-cysteine residues + a [DsbB protein] carrying a disulfide bond = a [DsbA protein] carrying a disulfide bond + a [DsbB protein] with reduced L-cysteine residues
(1a)
-
-
-
a [DsbB protein] with reduced L-cysteine residues + a quinone = a [DsbB protein] carrying a disulfide bond + a quinol
(1b)
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
protein dithiol:quinone oxidoreductase (disulfide-forming)
DsbB is a protein found in Gram-negative bacteria that functions within a pathway for protein disulfide bond formation. The enzyme catalyses the oxidation of the DsbA protein by generating disulfide bonds de novo via the reduction of membrane quinones. cf. EC 1.8.4.15, protein dithiol oxidoreductase (disulfide-forming).
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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
a [DsbA protein] with reduced L-cysteine residues + a quinone
a [DsbA protein] carrying a disulfide bond + a quinol
-
overall reaction
-
-
?
a [DsbA protein] with reduced L-cysteine residues + a [DsbB protein] carrying a disulfide bond
a [DsbA protein] carrying a disulfide bond + a [DsbB protein] with reduced L-cysteine residues
-
-
-
-
?
a [DsbA protein] with reduced L-cysteine residues + menaquinone
a [DsbA protein] carrying a disulfide bond + menaquinol
a [DsbA protein] with reduced L-cysteine residues + menaquinone-8
a [DsbA protein] carrying a disulfide bond + menaquinol-8
-
overall reaction
-
-
?
a [DsbA protein] with reduced L-cysteine residues + ubiquinone
a [DsbA protein] carrying a disulfide bond + ubiquinol
a [DsbA protein] with reduced L-cysteine residues + ubiquinone-1
a [DsbA protein] carrying a disulfide bond + ubiquinol-1
-
overall reaction
-
-
?
a [DsbB protein] with reduced L-cysteine residues + a quinone
a [DsbB protein] carrying a disulfide bond + a quinol
-
-
-
-
?
a [DsbB protein] with reduced L-cysteine residues + ubiquinone
a [DsbB protein] carrying a disulfide bond + ubiquinol
-
-
-
-
?
[DsbA protein] with reduced L-cysteine residues + a quinone
[DsbA protein] carrying a disulfide bond + a quinol
[DsbA protein] with reduced L-cysteine residues + menaquinone
[DsbA protein] carrying a disulfide bond + menaquinol
-
overall reaction
-
-
?
[DsbA protein] with reduced L-cysteine residues + quinone
[DsbA protein] carrying a disulfide bond + quinol
[DsbA protein] with reduced L-cysteine residues + ubiquinone
[DsbA protein] carrying a disulfide bond + ubiquinol
[DsbA protein] with reduced L-cysteine residues + ubiquinone Q8
[DsbA protein] carrying a disulfide bond + ubiquinol Q8
overall reaction
-
-
?
[DsbA protein] with reduced L-cysteine residues + ubiquinone-1
[DsbA protein] carrying a disulfide bond + ubiquinol-1
[DsbA protein] with reduced L-cysteine residues + ubiquinone-8
[DsbA protein] carrying a disulfide bond + ubiquinol-8
-
overall reaction
-
-
?
[DsbA protein] with reduced L-cysteine residues + [DsbB protein] carrying a disulfide bond
[DsbA protein] carrying a disulfide bond + [DsbB protein] with reduced L-cysteine residues
[DsbB protein] with reduced L-cysteine residues + a quinone
[DsbB protein] carrying a disulfide bond + a quinol
-
-
-
-
?
[DsbB protein] with reduced L-cysteine residues + ubiquinone
[DsbB protein] carrying a disulfide bond + ubiquinol
[DsbB protein] with reduced L-cysteine residues + ubiquinone-1
[DsbB protein] carrying a disulfide bond + ubiquinol-1
a [DsbA protein] with reduced L-cysteine residues + menaquinone
a [DsbA protein] carrying a disulfide bond + menaquinol
-
overall reaction
-
-
?
a [DsbA protein] with reduced L-cysteine residues + menaquinone
a [DsbA protein] carrying a disulfide bond + menaquinol
-
under unaerobic conditions, overall reaction
-
-
?
a [DsbA protein] with reduced L-cysteine residues + ubiquinone
a [DsbA protein] carrying a disulfide bond + ubiquinol
-
overall reaction
-
-
?
a [DsbA protein] with reduced L-cysteine residues + ubiquinone
a [DsbA protein] carrying a disulfide bond + ubiquinol
-
under aerobic conditions, overall reaction
-
-
?
[DsbA protein] with reduced L-cysteine residues + a quinone
[DsbA protein] carrying a disulfide bond + a quinol
-
overall reaction
-
-
?
[DsbA protein] with reduced L-cysteine residues + a quinone
[DsbA protein] carrying a disulfide bond + a quinol
-
overall reaction
-
-
?
[DsbA protein] with reduced L-cysteine residues + a quinone
[DsbA protein] carrying a disulfide bond + a quinol
-
overall reaction
-
-
?
[DsbA protein] with reduced L-cysteine residues + a quinone
[DsbA protein] carrying a disulfide bond + a quinol
-
overall reaction
-
-
?
[DsbA protein] with reduced L-cysteine residues + a quinone
[DsbA protein] carrying a disulfide bond + a quinol
-
overall reaction
-
-
?
[DsbA protein] with reduced L-cysteine residues + a quinone
[DsbA protein] carrying a disulfide bond + a quinol
-
overall reaction
-
-
?
[DsbA protein] with reduced L-cysteine residues + a quinone
[DsbA protein] carrying a disulfide bond + a quinol
-
overall reaction
-
-
?
[DsbA protein] with reduced L-cysteine residues + quinone
[DsbA protein] carrying a disulfide bond + quinol
overall reaction
-
-
?
[DsbA protein] with reduced L-cysteine residues + quinone
[DsbA protein] carrying a disulfide bond + quinol
overall reaction
-
-
?
[DsbA protein] with reduced L-cysteine residues + ubiquinone
[DsbA protein] carrying a disulfide bond + ubiquinol
-
overall reaction
-
-
?
[DsbA protein] with reduced L-cysteine residues + ubiquinone
[DsbA protein] carrying a disulfide bond + ubiquinol
overall reaction
-
-
?
[DsbA protein] with reduced L-cysteine residues + ubiquinone-1
[DsbA protein] carrying a disulfide bond + ubiquinol-1
overall reaction
-
-
?
[DsbA protein] with reduced L-cysteine residues + ubiquinone-1
[DsbA protein] carrying a disulfide bond + ubiquinol-1
overall reaction
-
-
?
[DsbA protein] with reduced L-cysteine residues + ubiquinone-1
[DsbA protein] carrying a disulfide bond + ubiquinol-1
overall reaction
-
-
?
[DsbA protein] with reduced L-cysteine residues + ubiquinone-1
[DsbA protein] carrying a disulfide bond + ubiquinol-1
overall reaction
-
-
?
[DsbA protein] with reduced L-cysteine residues + ubiquinone-1
[DsbA protein] carrying a disulfide bond + ubiquinol-1
-
overall reaction
-
-
?
[DsbA protein] with reduced L-cysteine residues + [DsbB protein] carrying a disulfide bond
[DsbA protein] carrying a disulfide bond + [DsbB protein] with reduced L-cysteine residues
-
-
-
?
[DsbA protein] with reduced L-cysteine residues + [DsbB protein] carrying a disulfide bond
[DsbA protein] carrying a disulfide bond + [DsbB protein] with reduced L-cysteine residues
-
-
-
?
[DsbA protein] with reduced L-cysteine residues + [DsbB protein] carrying a disulfide bond
[DsbA protein] carrying a disulfide bond + [DsbB protein] with reduced L-cysteine residues
-
-
-
-
?
[DsbA protein] with reduced L-cysteine residues + [DsbB protein] carrying a disulfide bond
[DsbA protein] carrying a disulfide bond + [DsbB protein] with reduced L-cysteine residues
-
-
-
?
[DsbB protein] with reduced L-cysteine residues + ubiquinone
[DsbB protein] carrying a disulfide bond + ubiquinol
-
-
-
-
?
[DsbB protein] with reduced L-cysteine residues + ubiquinone
[DsbB protein] carrying a disulfide bond + ubiquinol
-
-
-
?
[DsbB protein] with reduced L-cysteine residues + ubiquinone-1
[DsbB protein] carrying a disulfide bond + ubiquinol-1
-
-
-
?
[DsbB protein] with reduced L-cysteine residues + ubiquinone-1
[DsbB protein] carrying a disulfide bond + ubiquinol-1
-
-
-
?
additional information
?
-
-
membranes containing CtDsbB can sustain CtDsbA catalysed oxidation of a model substrate. Detergent solubilised, purified CtDsbB partially oxidises reduced CtDsbA, the active site CSAC thiols are the likely target for CtDsbB mediated oxidation
-
-
-
additional information
?
-
membranes containing CtDsbB can sustain CtDsbA catalysed oxidation of a model substrate. Detergent solubilised, purified CtDsbB partially oxidises reduced CtDsbA, the active site CSAC thiols are the likely target for CtDsbB mediated oxidation
-
-
-
additional information
?
-
membranes containing CtDsbB can sustain CtDsbA catalysed oxidation of a model substrate. Detergent solubilised, purified CtDsbB partially oxidises reduced CtDsbA, the active site CSAC thiols are the likely target for CtDsbB mediated oxidation
-
-
-
additional information
?
-
-
reduced DsbA forms a complex with the enzyme in which Cys30 of DsbA is disulfide-bonded to Cys104 of the enzyme. Cys104 is rapidly replaced by Cys33 of DsbA to generate the oxidized form of this protein
-
-
-
additional information
?
-
-
the enzyme is initially oxidized (state A). Disulfide interaction between Cys30 of DsbA protein and Cys104 of the enzyme then triggers the recycling reaction of DsbA (state B), allowing over all electron transfer from newly secreted protein via DsbA (Cys30/Cys33) to the enzyme in which intra-chain electron flow from Cys104/Cys130 (state C) to Cys41/Cys44 (state D) may occur
-
-
-
additional information
?
-
-
enzyme-catalyzed DsbA protein oxidation is an entropy-driven reaction originating from delocalization of electrons among four cysteine residues in the enzyme, which proceeds independently of an oxidizing power of ubiquinone
-
-
-
additional information
?
-
-
mutant DsbA protein C33S preferentially forms mixed disulfides with the enzyme
-
-
-
additional information
?
-
-
the enzyme gains the ability to oxidize its specific substrate, DsbA protein, having very high redox potential, by undergoing a DsbA-induced rearrangement of cysteine residues. One of the enzyme cysteines that are now reduced then interacts with ubiquinone to form a charge transfer complex, leading to the regeneration of a disulfide at the enzyme active site
-
-
-
additional information
?
-
-
the enzyme uses its two pairs of cysteines in a coordinated reaction to accept electrons from the active cysteines in DsbA protein
-
-
-
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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
a [DsbA protein] with reduced L-cysteine residues + a quinone
a [DsbA protein] carrying a disulfide bond + a quinol
-
overall reaction
-
-
?
a [DsbA protein] with reduced L-cysteine residues + a [DsbB protein] carrying a disulfide bond
a [DsbA protein] carrying a disulfide bond + a [DsbB protein] with reduced L-cysteine residues
-
-
-
-
?
a [DsbA protein] with reduced L-cysteine residues + menaquinone
a [DsbA protein] carrying a disulfide bond + menaquinol
-
under unaerobic conditions, overall reaction
-
-
?
a [DsbA protein] with reduced L-cysteine residues + ubiquinone
a [DsbA protein] carrying a disulfide bond + ubiquinol
a [DsbB protein] with reduced L-cysteine residues + a quinone
a [DsbB protein] carrying a disulfide bond + a quinol
-
-
-
-
?
a [DsbB protein] with reduced L-cysteine residues + ubiquinone
a [DsbB protein] carrying a disulfide bond + ubiquinol
-
-
-
-
?
[DsbA protein] with reduced L-cysteine residues + a quinone
[DsbA protein] carrying a disulfide bond + a quinol
[DsbA protein] with reduced L-cysteine residues + menaquinone
[DsbA protein] carrying a disulfide bond + menaquinol
-
overall reaction
-
-
?
[DsbA protein] with reduced L-cysteine residues + quinone
[DsbA protein] carrying a disulfide bond + quinol
[DsbA protein] with reduced L-cysteine residues + ubiquinone
[DsbA protein] carrying a disulfide bond + ubiquinol
[DsbA protein] with reduced L-cysteine residues + ubiquinone Q8
[DsbA protein] carrying a disulfide bond + ubiquinol Q8
overall reaction
-
-
?
[DsbA protein] with reduced L-cysteine residues + ubiquinone-1
[DsbA protein] carrying a disulfide bond + ubiquinol-1
[DsbA protein] with reduced L-cysteine residues + [DsbB protein] carrying a disulfide bond
[DsbA protein] carrying a disulfide bond + [DsbB protein] with reduced L-cysteine residues
[DsbB protein] with reduced L-cysteine residues + a quinone
[DsbB protein] carrying a disulfide bond + a quinol
-
-
-
-
?
[DsbB protein] with reduced L-cysteine residues + ubiquinone
[DsbB protein] carrying a disulfide bond + ubiquinol
[DsbB protein] with reduced L-cysteine residues + ubiquinone-1
[DsbB protein] carrying a disulfide bond + ubiquinol-1
a [DsbA protein] with reduced L-cysteine residues + ubiquinone
a [DsbA protein] carrying a disulfide bond + ubiquinol
-
overall reaction
-
-
?
a [DsbA protein] with reduced L-cysteine residues + ubiquinone
a [DsbA protein] carrying a disulfide bond + ubiquinol
-
under aerobic conditions, overall reaction
-
-
?
[DsbA protein] with reduced L-cysteine residues + a quinone
[DsbA protein] carrying a disulfide bond + a quinol
-
overall reaction
-
-
?
[DsbA protein] with reduced L-cysteine residues + a quinone
[DsbA protein] carrying a disulfide bond + a quinol
-
overall reaction
-
-
?
[DsbA protein] with reduced L-cysteine residues + a quinone
[DsbA protein] carrying a disulfide bond + a quinol
-
overall reaction
-
-
?
[DsbA protein] with reduced L-cysteine residues + a quinone
[DsbA protein] carrying a disulfide bond + a quinol
-
overall reaction
-
-
?
[DsbA protein] with reduced L-cysteine residues + a quinone
[DsbA protein] carrying a disulfide bond + a quinol
-
overall reaction
-
-
?
[DsbA protein] with reduced L-cysteine residues + a quinone
[DsbA protein] carrying a disulfide bond + a quinol
-
overall reaction
-
-
?
[DsbA protein] with reduced L-cysteine residues + a quinone
[DsbA protein] carrying a disulfide bond + a quinol
-
overall reaction
-
-
?
[DsbA protein] with reduced L-cysteine residues + quinone
[DsbA protein] carrying a disulfide bond + quinol
overall reaction
-
-
?
[DsbA protein] with reduced L-cysteine residues + quinone
[DsbA protein] carrying a disulfide bond + quinol
overall reaction
-
-
?
[DsbA protein] with reduced L-cysteine residues + ubiquinone
[DsbA protein] carrying a disulfide bond + ubiquinol
-
overall reaction
-
-
?
[DsbA protein] with reduced L-cysteine residues + ubiquinone
[DsbA protein] carrying a disulfide bond + ubiquinol
overall reaction
-
-
?
[DsbA protein] with reduced L-cysteine residues + ubiquinone-1
[DsbA protein] carrying a disulfide bond + ubiquinol-1
overall reaction
-
-
?
[DsbA protein] with reduced L-cysteine residues + ubiquinone-1
[DsbA protein] carrying a disulfide bond + ubiquinol-1
overall reaction
-
-
?
[DsbA protein] with reduced L-cysteine residues + [DsbB protein] carrying a disulfide bond
[DsbA protein] carrying a disulfide bond + [DsbB protein] with reduced L-cysteine residues
-
-
-
?
[DsbA protein] with reduced L-cysteine residues + [DsbB protein] carrying a disulfide bond
[DsbA protein] carrying a disulfide bond + [DsbB protein] with reduced L-cysteine residues
-
-
-
?
[DsbA protein] with reduced L-cysteine residues + [DsbB protein] carrying a disulfide bond
[DsbA protein] carrying a disulfide bond + [DsbB protein] with reduced L-cysteine residues
-
-
-
-
?
[DsbA protein] with reduced L-cysteine residues + [DsbB protein] carrying a disulfide bond
[DsbA protein] carrying a disulfide bond + [DsbB protein] with reduced L-cysteine residues
-
-
-
?
[DsbB protein] with reduced L-cysteine residues + ubiquinone
[DsbB protein] carrying a disulfide bond + ubiquinol
-
-
-
-
?
[DsbB protein] with reduced L-cysteine residues + ubiquinone
[DsbB protein] carrying a disulfide bond + ubiquinol
-
-
-
?
[DsbB protein] with reduced L-cysteine residues + ubiquinone-1
[DsbB protein] carrying a disulfide bond + ubiquinol-1
-
-
-
?
[DsbB protein] with reduced L-cysteine residues + ubiquinone-1
[DsbB protein] carrying a disulfide bond + ubiquinol-1
-
-
-
?
additional information
?
-
-
reduced DsbA forms a complex with the enzyme in which Cys30 of DsbA is disulfide-bonded to Cys104 of the enzyme. Cys104 is rapidly replaced by Cys33 of DsbA to generate the oxidized form of this protein
-
-
-
additional information
?
-
-
the enzyme is initially oxidized (state A). Disulfide interaction between Cys30 of DsbA protein and Cys104 of the enzyme then triggers the recycling reaction of DsbA (state B), allowing over all electron transfer from newly secreted protein via DsbA (Cys30/Cys33) to the enzyme in which intra-chain electron flow from Cys104/Cys130 (state C) to Cys41/Cys44 (state D) may occur
-
-
-
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3'-bromo-1-methyl-5-oxo[1,2,5,6-tetrahydro[1,1'-biphenyl]]-3-yl propanoate
-
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
O2
-
the oxidation of DsbA by the enzyme strongly depends on the presence of oxygen
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Tuberculosis
Inhibition of bacterial disulfide bond formation by the anticoagulant warfarin.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0011
3'-bromo-1-methyl-5-oxo[1,2,5,6-tetrahydro[1,1'-biphenyl]]-3-yl propanoate
Escherichia coli
-
pH and temperature not specified in the publication
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
-
the enzyme facilitates the formation of disulfide bonds in periplasmic proteins but does not facilitate the formation of intramembraneous disulfides
physiological function
malfunction
-
mutation in the DsbA-enzyme system results in an increase in sensitivity to Cd2+ and Zn2+ as well as a variety of antibiotics including beta-lactams, kanamycin, erythromycin, novobiocin, ofloxacin and sodium dodecyl sulfate
malfunction
-
mutation in the DsbA-enzyme system results in an increase in sensitivity to Cd2+ and Zn2+ as well as a variety of antibiotics including beta-lactams, kanamycin, erythromycin, novobiocin, ofloxacin and sodium dodecyl sulfate
-
physiological function
the enzyme is required for virulence in Burkholderia pseudomallei
physiological function
the enzyme oxidizes DsbA for continuous protein disulfide bond formation in the cell
physiological function
disulfide bond protein A (DsbA) is the primary oxidase in the disulfide oxidative pathway of bacteria. DsbA catalyses the introduction of disulfide bonds into reduced and folding proteins in concert with a membrane protein partner DsbB. DsbB uses a quinone cofactor as an electron acceptor, and together the DsbA-DsbB pair ultimately shuttle electrons from a reduced protein substrate to molecular oxygen via the respiratory pathway. CtDsbA is directly oxidised by CtDsbB, in a reaction in which both periplasmic cysteine pairs of CtDsbB are required for complete activity. The second disulfide of CtDsbA does not influence interaction with CtDsbB
physiological function
-
the enzyme is required for virulence in Burkholderia pseudomallei
-
physiological function
-
disulfide bond protein A (DsbA) is the primary oxidase in the disulfide oxidative pathway of bacteria. DsbA catalyses the introduction of disulfide bonds into reduced and folding proteins in concert with a membrane protein partner DsbB. DsbB uses a quinone cofactor as an electron acceptor, and together the DsbA-DsbB pair ultimately shuttle electrons from a reduced protein substrate to molecular oxygen via the respiratory pathway. CtDsbA is directly oxidised by CtDsbB, in a reaction in which both periplasmic cysteine pairs of CtDsbB are required for complete activity. The second disulfide of CtDsbA does not influence interaction with CtDsbB
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). G4NNC5_CHLT4
Chlamydia trachomatis serovar A (strain A2497)
135
0
15005
TrEMBL
Secretory Pathway (Reliability: 1)
DSBB_ECOLI
Escherichia coli (strain K12)
176
0
20142
Swiss-Prot
other Location (Reliability: 5)
DSBB_BURPS
Burkholderia pseudomallei (strain K96243)
169
0
18114
Swiss-Prot
-
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme complexed with ubiquinone Q8 and DsbA, sitting drop vapor diffusion method, using 30% (w/v) PEG 550MME, 0.3 M ammonium formate and 0.05 M Tris/HCl, pH 8.9
sitting drop vapor diffusion method, using 15% (w/v) PEG3350, 0.1M magnesium formate and 0.1M MOPS (pH 7.0)
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C41A/C44A
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the mutant has two cysteine residues at Cys104 and Cys130 compared to the wild type enzyme with Cys41, Cys44, Cys104 and Cys130
R48H
Y46P/E47P
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the mutant shows strongly reduced DsbA protein oxidation activity
additional information
additional information
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construction of mutant CtDsbB-CCSS, in which periplasmic loop 2 Cys98 and Cys104 are mutated to serines. In the presence of CtDsbB-CCSS or CtDsbB-SSCC, CtDsbA catalysed oxidation of the peptide substrate is markedly reduced relative to wild-type CtDsbB, although oxidation proceeds more rapidly than observed for negative controls containing only buffer, or the wild-type CtDsbB variant alone. The disulfide bonds present in periplasmic loops P1 and P2 of CtDsbB are each required for complete oxidation of CtDsbA
additional information
construction of mutant CtDsbB-CCSS, in which periplasmic loop 2 Cys98 and Cys104 are mutated to serines. In the presence of CtDsbB-CCSS or CtDsbB-SSCC, CtDsbA catalysed oxidation of the peptide substrate is markedly reduced relative to wild-type CtDsbB, although oxidation proceeds more rapidly than observed for negative controls containing only buffer, or the wild-type CtDsbB variant alone. The disulfide bonds present in periplasmic loops P1 and P2 of CtDsbB are each required for complete oxidation of CtDsbA
additional information
-
construction of mutant CtDsbB-CCSS, in which periplasmic loop 2 Cys98 and Cys104 are mutated to serines. In the presence of CtDsbB-CCSS or CtDsbB-SSCC, CtDsbA catalysed oxidation of the peptide substrate is markedly reduced relative to wild-type CtDsbB, although oxidation proceeds more rapidly than observed for negative controls containing only buffer, or the wild-type CtDsbB variant alone. The disulfide bonds present in periplasmic loops P1 and P2 of CtDsbB are each required for complete oxidation of CtDsbA
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HisTrap nickel affinity column chromatography and Superdex S200 gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed with the biotin carboxyl carrier protein tag in Escherichia coli C41 (DE3) cells
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gene dsbB, recombinant expression of recombinant enzyme in Escherichia coli, coexpression with Chlamydia trachomatis dsbA
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
CtDsbA protein is detected in Chlamydia trachomatis inclusion vacuoles at 20 h post infection, with more detected at 32 and similar levels at 44 h post infection as the developmental cycle proceeds
CtDsbA protein is detected in Chlamydia trachomatis inclusion vacuoles at 20 h post infection, with more detected at 32 and similar levels at 44 h post infection as the developmental cycle proceeds
CtDsbA protein is detected in Chlamydia trachomatis inclusion vacuoles at 20 h post infection, with more detected at 32 and similar levels at 44 h post infection as the developmental cycle proceeds
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Borsetti, F.; Francia, F.; Turner, R.J.; Zannoni, D.
The thiol:disulfide oxidoreductase DsbB mediates the oxidizing effects of the toxic metalloid tellurite (TeO32-) on the plasma membrane redox system of the facultative phototroph Rhodobacter capsulatus