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a [protein] carrying a disulfide bond + thioredoxin
a [protein] with reduced L-cysteine residues + thioredoxin disulfide
a [protein] carrying a disulfide bond + thioredoxin-1
a [protein] with reduced L-cysteine residues + thioredoxin-1 disulfide
-
overall reaction
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-
?
a [protein] with reduced L-cysteine residues + thioredoxin disulfide
a [protein] carrying a disulfide bond + thioredoxin
CQQGFDGTQNSCK peptide containing amide-coupled tetraazacyclododecane-1,4,7,10-tetraacetic acid + GSSG
?
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?
human insulin + reduced dithiothreitol
?
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-
-
-
?
insulin + dithiothreitol
reduced insulin + oxidized dithiothreitol
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-
-
-
?
[CcmG protein] carrying a disulfide bond + thioredoxin
[CcmG protein] with reduced L-cysteine residues + thioredoxin disulfide
[DsbC protein] carrying a disulfide bond + thioredoxin
[DsbC protein] with reduced L-cysteine residues + thioredoxin disulfide
[DsbC protein] carrying a disulfide bond + thioredoxin
[DsbC] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
-
?
[DsbC protein] with reduced L-cysteine residues + thioredoxin disulfide
[DsbC protein] carrying a disulfide bond + thioredoxin
-
-
-
-
?
[DsbE protein] carrying a disulfide bond + thioredoxin
[DsbE protein] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
?
[DsbG protein] carrying a disulfide bond + thioredoxin
[DsbG protein] with reduced L-cysteine residues + thioredoxin disulfide
[DsbG protein] with reduced L-cysteine residues + thioredoxin disulfide
[DsbG protein] carrying a disulfide bond + thioredoxin
-
-
-
-
?
[HelX protein] carrying a disulfide bond + thioredoxin
[HelX protein] with reduced L-cysteine residues + thioredoxin disulfide
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-
-
-
?
[protein DsbC] carrying a disulfide bond + thioredoxin
[protein DsbC] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
-
-
[protein DsbE] carrying a disulfide bond + thioredoxin
[protein DsbE] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
-
-
[protein DsbG] carrying a disulfide bond + thioredoxin
[protein DsbG] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
-
-
additional information
?
-
a [protein] carrying a disulfide bond + thioredoxin

a [protein] with reduced L-cysteine residues + thioredoxin disulfide
-
overall reaction
-
-
?
a [protein] carrying a disulfide bond + thioredoxin
a [protein] with reduced L-cysteine residues + thioredoxin disulfide
-
overall reaction
?
-
-
a [protein] with reduced L-cysteine residues + thioredoxin disulfide

a [protein] carrying a disulfide bond + thioredoxin
-
overall reaction
-
-
?
a [protein] with reduced L-cysteine residues + thioredoxin disulfide
a [protein] carrying a disulfide bond + thioredoxin
-
overall reaction
-
-
?
a [protein] with reduced L-cysteine residues + thioredoxin disulfide
a [protein] carrying a disulfide bond + thioredoxin
-
overall reaction
-
-
?
[CcmG protein] carrying a disulfide bond + thioredoxin

[CcmG protein] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
-
?
[CcmG protein] carrying a disulfide bond + thioredoxin
[CcmG protein] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
-
?
[DsbC protein] carrying a disulfide bond + thioredoxin

[DsbC protein] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
-
?
[DsbC protein] carrying a disulfide bond + thioredoxin
[DsbC protein] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
?
[DsbC protein] carrying a disulfide bond + thioredoxin
[DsbC protein] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
-
?
[DsbG protein] carrying a disulfide bond + thioredoxin

[DsbG protein] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
-
?
[DsbG protein] carrying a disulfide bond + thioredoxin
[DsbG protein] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
?
[DsbG protein] carrying a disulfide bond + thioredoxin
[DsbG protein] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
-
?
additional information

?
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-
electron transfer by the enzyme involves sequential reduction and oxidation of its three structural domains, in which reducing potential is transferred from cytoplasmic thioredoxin to the beta domain, then successively to gamma and alpha, and thence to periplasmic substrates. Formation of a disulfide bond between cysteines 163 and 285 of the beta domain is part of the mechanism of the transmembrane electron transfer by the enzyme
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-
-
additional information
?
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the enzyme does not catalyze the reduction of the disulfide of the thioredoxin-like oxidant DsbA
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-
-
additional information
?
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the enzyme includes three domains, each containing a pair of cysteine residues that perform a series of disulfide exchange reactions. In the first step, the transmembrane domain accepts electrons from thioredoxin in the cytoplasm; these are then transferred to the periplasmic C-terminal domain and finally to the N-terminal domain, which is also located in the periplasm
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-
-
additional information
?
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-
the enzyme is composed of three domains, each containing two redox-active cysteines. All six of these cysteines are required for enzyme activity. The N-terminal periplasmic domain DsbDalpha directly reduces DsbC. DsbDalpha is then itself reduced by the C-terminal periplasmic domain, DsbDgamma, a thioredoxin-like polypeptide. The resulting oxidized DsbDgamma is reduced by the membrane-embedded DsbDbeta domain that contains eight transmembrane segments. Electrons passed from cytoplasmic thioredoxin 1 restore DsbDbeta to the reduced form, thus allowing it to continue to transfer electrons to DsbDgamma
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-
additional information
?
-
the enzyme transfers reducing power from the cytoplasm to the periplasm so as to facilitate the formation of correct disulphide bonds and c-type cytochromes in the latter compartment
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-
-
additional information
?
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the enzyme transports electrons without using a metabolite or a cofactor
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-
-
additional information
?
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the periplasmic protein TrbB relies on the enzyme from Escherichia coli for maintenance of its C-X-X-C redox active site motif which is responsible for its enzymatic activity
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a [protein] carrying a disulfide bond + thioredoxin
a [protein] with reduced L-cysteine residues + thioredoxin disulfide
a [protein] carrying a disulfide bond + thioredoxin-1
a [protein] with reduced L-cysteine residues + thioredoxin-1 disulfide
-
overall reaction
-
-
?
a [protein] with reduced L-cysteine residues + thioredoxin disulfide
a [protein] carrying a disulfide bond + thioredoxin
[CcmG protein] carrying a disulfide bond + thioredoxin
[CcmG protein] with reduced L-cysteine residues + thioredoxin disulfide
[DsbC protein] carrying a disulfide bond + thioredoxin
[DsbC protein] with reduced L-cysteine residues + thioredoxin disulfide
[DsbC protein] carrying a disulfide bond + thioredoxin
[DsbC] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
-
?
[DsbC protein] with reduced L-cysteine residues + thioredoxin disulfide
[DsbC protein] carrying a disulfide bond + thioredoxin
-
-
-
-
?
[DsbE protein] carrying a disulfide bond + thioredoxin
[DsbE protein] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
?
[DsbG protein] carrying a disulfide bond + thioredoxin
[DsbG protein] with reduced L-cysteine residues + thioredoxin disulfide
[DsbG protein] with reduced L-cysteine residues + thioredoxin disulfide
[DsbG protein] carrying a disulfide bond + thioredoxin
-
-
-
-
?
[HelX protein] carrying a disulfide bond + thioredoxin
[HelX protein] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
-
?
[protein DsbC] carrying a disulfide bond + thioredoxin
[protein DsbC] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
-
-
[protein DsbE] carrying a disulfide bond + thioredoxin
[protein DsbE] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
-
-
[protein DsbG] carrying a disulfide bond + thioredoxin
[protein DsbG] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
-
-
a [protein] carrying a disulfide bond + thioredoxin

a [protein] with reduced L-cysteine residues + thioredoxin disulfide
-
overall reaction
-
-
?
a [protein] carrying a disulfide bond + thioredoxin
a [protein] with reduced L-cysteine residues + thioredoxin disulfide
-
overall reaction
?
-
-
a [protein] with reduced L-cysteine residues + thioredoxin disulfide

a [protein] carrying a disulfide bond + thioredoxin
-
overall reaction
-
-
?
a [protein] with reduced L-cysteine residues + thioredoxin disulfide
a [protein] carrying a disulfide bond + thioredoxin
-
overall reaction
-
-
?
a [protein] with reduced L-cysteine residues + thioredoxin disulfide
a [protein] carrying a disulfide bond + thioredoxin
-
overall reaction
-
-
?
[CcmG protein] carrying a disulfide bond + thioredoxin

[CcmG protein] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
-
?
[CcmG protein] carrying a disulfide bond + thioredoxin
[CcmG protein] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
-
?
[DsbC protein] carrying a disulfide bond + thioredoxin

[DsbC protein] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
-
?
[DsbC protein] carrying a disulfide bond + thioredoxin
[DsbC protein] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
?
[DsbC protein] carrying a disulfide bond + thioredoxin
[DsbC protein] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
-
?
[DsbG protein] carrying a disulfide bond + thioredoxin

[DsbG protein] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
-
?
[DsbG protein] carrying a disulfide bond + thioredoxin
[DsbG protein] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
?
[DsbG protein] carrying a disulfide bond + thioredoxin
[DsbG protein] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
-
?
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malfunction

-
enzyme absence enhances the sensitivity of the dsbA1A2 mutant to oxidative stress
malfunction
-
enzyme loss leads to hypersensitivity to dithiothreitol and benzylpenicillin
malfunction
-
enzyme absence enhances the sensitivity of the dsbA1A2 mutant to oxidative stress
-
metabolism

-
cytoplasmic electrons donated by thioredoxin are transferred into the periplasm via the enzyme
metabolism
-
the enzyme accepts electrons from cytoplasmic thioredoxin and shuttles these electrons via a well-defined cascade through the membrane-spanning region and into the periplasm
metabolism
-
the enzyme generates a reducing source in the periplasm, which is required for maintaining proper redox conditions
metabolism
-
the enzyme is a reductase that acts as an electron hub, translocating reducing equivalents from cytoplasmic thioredoxin to a number of periplasmic substrates involved in oxidative protein folding, cytochrome c maturation and oxidative stress defence
metabolism
-
the enzyme is involved only in cytochromexa0c biogenesis
metabolism
-
the enzyme is required to maintain the functional oxidation state of DsbC and DsbG
metabolism
-
the enzyme mediates electron transfer from the cytoplasm across the membrane
metabolism
-
the enzyme transfers reducing potential to periplasmic protein disulfide bond isomerases and to the cytochromexa0c thioreduction pathway
metabolism
-
the enzyme is a reductase that acts as an electron hub, translocating reducing equivalents from cytoplasmic thioredoxin to a number of periplasmic substrates involved in oxidative protein folding, cytochrome c maturation and oxidative stress defence
-
physiological function

-
overproduction of the enzyme and protein disulfide isomerase DsbC markedly enhances periplasmic production of human nerve growth factor in Escherichia coli
physiological function
-
the enzyme is essential for bacterial growth at temperatures above 42°C
physiological function
-
the enzyme is essential for survival of Neisseria gonorrhoeae
physiological function
-
the enzyme is required for the survival Neisseria meningitides
physiological function
NmDsbD is essential for viability. To initiate electron transport across the inner membrane, the disulfide bonded cysteine residues in t-DsbD are reduced by cytoplasmic thioredoxin. The transmebrane part, t-DsbD, in turn reduces the disulfide bond in c-DsbD, which then reduces n-DsbD. Lastly, n-DsbD transfers electrons to periplasmic substrates including the isomerases DsbC and DsbG, which reshuffle non-native disulfide bonds in multi-cysteine containing, as well as the reductases CcmG (DsbE), and CcmH which are involved in cytochrome c maturation
physiological function
-
the enzyme is required for the survival Neisseria meningitides
-
physiological function
-
NmDsbD is essential for viability. To initiate electron transport across the inner membrane, the disulfide bonded cysteine residues in t-DsbD are reduced by cytoplasmic thioredoxin. The transmebrane part, t-DsbD, in turn reduces the disulfide bond in c-DsbD, which then reduces n-DsbD. Lastly, n-DsbD transfers electrons to periplasmic substrates including the isomerases DsbC and DsbG, which reshuffle non-native disulfide bonds in multi-cysteine containing, as well as the reductases CcmG (DsbE), and CcmH which are involved in cytochrome c maturation
-
additional information

13Calpha and 13Cbeta chemical shift comparison of the two active site cysteine residues between n-NmDsbDOx and n-NmDsbDRed relative to the average BMRB shift values, overview
additional information
-
13Calpha and 13Cbeta chemical shift comparison of the two active site cysteine residues between n-NmDsbDOx and n-NmDsbDRed relative to the average BMRB shift values, overview
-
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Smith, R.; Whitten, A.; Paxman, J.; Kahler, C.; Scanlon, M.; Heras, B.
Production, biophysical characterization and initial crystallization studies of the N- and C-terminal domains of DsbD, an essential enzyme in Neisseria meningitidis
Acta Crystallogr. Sect. F
74
31-38
2018
Neisseria meningitidis, Neisseria meningitidis NMB
brenda
Goulding, C.; Sawaya, M.; Parseghian, A.; Lim, V.; Eisenberg, D.; Missiakas, D.
Thiol-disulfide exchange in an immunoglobulin-like fold Structure of the N-terminal domain of DsbD
Biochemistry
41
6920-6927
2002
Escherichia coli (P36655)
brenda
Quinternet, M.; Tsan, P.; Selme, L.; Beaufils, C.; Jacob, C.; Boschi-Muller, S.; Averlant-Petit, M.; Branlant, G.; Cung, M.
Solution structure and backbone dynamics of the cysteine 103 to serine mutant of the N-terminal domain of DsbD from Neisseria meningitides
Biochemistry
47
12710-12720
2008
Neisseria meningitidis
brenda
Mavridou, D.; Stelzl, L.; Ferguson, S.; Redfield, C.
1H, 13C and 15N resonance assignments for the oxidized and reduced states of the N-terminal domain of DsbD from Escherichia coli
Biomol. NMR Assign.
6
163-167
2012
Escherichia coli
brenda
Katzen, F.; Beckwith, J.
Transmembrane electron transfer by the membrane protein DsbD occurs via a disulfide bond cascade
Cell
103
769-779
2000
Escherichia coli
brenda
Missiakas, D.; Schwager, F.; Raina, S.
Identification and charactcerization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli
EMBO J.
14
3415-3424
1995
Escherichia coli
brenda
Stewart, E.; Katzen, F.; Beckwith, J.
Six conserved cysteines of the membrane protein DsbD are required for the transfer of electrons from the cytoplasm to the periplasm of Escherichia coli
EMBO J.
18
5963-5971
1999
Escherichia coli
brenda
Katzen, F.; Deshmukh, M.; Daldal, F.; Beckwith, J.
Evolutionary domain fusion expanded the substrate specificity of the transmembrane electron transporter DsbD
EMBO J.
21
3960-3969
2002
Escherichia coli, Rhodobacter capsulatus
brenda
Cho, S.; Porat, A.; Ye, J.; Beckwith, J.
Redox-active cysteines of a membrane electron transporter DsbD show dual compartment accessibility
EMBO J.
26
3509-3520
2007
Escherichia coli
brenda
Hiniker, A.; Vertommen, D.; Bardwell, J.; Collet, J.
Evidence for conformational changes within DsbD Possible role for membrane-embedded proline residues
J. Bacteriol.
188
7317-7320
2006
Escherichia coli
brenda
Hemmis, C.; Berkmen, M.; Eser, M.; Schildbach, J.
TrbB from conjugative plasmid F is a structurally distinct disulfide isomerase that requires DsbD for redox state maintenance
J. Bacteriol.
193
4588-4597
2011
Escherichia coli
brenda
Kurokawa, Y.; Yanagi, H.; Yura, T.
Overproduction of bacterial protein disulfide isomerase (DsbC) and its modulator (DsbD) markedly enhances periplasmic production of human nerve growth factor in Escherichia coli
J. Biol. Chem.
276
14393-14399
2001
Escherichia coli
-
brenda
Krupp, R.; Chan, C.; Missiakas, D.
DsbD-catalyzed transport of electrons across the membrane of Escherichia coli
J. Biol. Chem.
276
3696-3701
2001
Escherichia coli
brenda
Cho, S.; Beckwith, J.
Two snapshots of electron transport across the membrane Insights into the structure and function of DsbD
J. Biol. Chem.
284
11416-11424
2009
Escherichia coli
brenda
Mavridou, D.; Stevens, J.; Goddard, A.; Willis, A.; Ferguson, S.; Redfield, C.
Control of periplasmic interdomain thiol disulfide exchange in the transmembrane oxidoreductase DsbD
J. Biol. Chem.
284
3219-3226
2009
Escherichia coli
brenda
Smith, R.; Mohanty, B.; Mowlaboccus, S.; Paxman, J.; Williams, M.; Headey, S.; Wang, G.; Subedi, P.; Doak, B.; Kahler, C.; Scanlon, M.; Heras, B.
Structural and biochemical insights into the disulfide reductase mechanism of DsbD, an essential enzyme for neisserial pathogens
J. Biol. Chem.
293
16559-16571
2018
Neisseria gonorrhoeae
brenda
Mavridou, D.; Stevens, J.; Ferguson, S.; Redfield, C.
Active-site properties of the oxidized and reduced C-terminal domain of DsbD obtained by NMR spectroscopy
J. Mol. Biol.
370
643-658
2007
Escherichia coli
brenda
Chung, J.; Chen, T.; Missiakas, D.
Transfer of electrons across the cytoplasmic membrane by DsbD, a membrane protein involved in thiol-disulphide exchange and protein folding in the bacterial periplasm
Mol. Microbiol.
35
1099-1109
2000
Escherichia coli
brenda
Gordon, E.; Page, M.; Willis, A.; Ferguson, S.
Escherichia coli DipZ Anatomy of a transmembrane protein disulphide reductase in which three pairs of cysteine residues, one in each of three domains, contribute differentially to function
Mol. Microbiol.
35
1360-1374
2000
Escherichia coli (P36655)
brenda
Kumar, P.; Sannigrahi, S.; Scoullar, J.; Kahler, C.; Tzeng, Y.
Characterization of DsbD in Neisseria meningitidis
Mol. Microbiol.
79
1557-1573
2011
Neisseria meningitidis, Neisseria meningitidis CDC 8201085
brenda
Katzen, F.; Beckwith, J.
Role and location of the unusual redox-active cysteines in the hydrophobic domain of the transmembrane electron transporter DsbD
Proc. Natl. Acad. Sci. USA
100
10471-10476
2003
Escherichia coli
brenda
Goldstone, D.; Haebel, P.; Katzen, F.; Bader, M.; Bardwell, J.; Beckwith, J.; Metcalf, P.
DsbC activation by the N-terminal domain of DsbD
Proc. Natl. Acad. Sci. USA
98
9551-9556
2001
Escherichia coli
brenda
Smith, R.; Mohanty, B.; Williams, M.; Scanlon, M.; Heras, B.
HN, N, Calpha and Cbeta assignments of the two periplasmic domains of Neisseria meningitidis DsbD
Biomol. NMR Assign.
11
181-186
2017
Neisseria meningitidis (Q9JYM0), Neisseria meningitidis NMB (Q9JYM0)
brenda