DB code: D00278

CATH domain 3.10.450.70 : Nuclear Transport Factor 2; Chain
3.40.30.10 : Glutaredoxin Catalytic domain
E.C. 5.3.4.1
CSA 1eej
M-CSA 1eej
MACiE

CATH domain Related DB codes (homologues)
3.40.30.10 : Glutaredoxin S00916 S00279 M00184 D00866 D00869 D00870

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P0AEG6 Thiol:disulfide interchange protein dsbC
None NP_417369.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_491094.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
PF10411 (DsbC_N)
PF13098 (Thioredoxin_2)
[Graphical View]

KEGG enzyme name
protein disulfide-isomerase
S-S rearrangase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P0AEG6 DSBC_ECOLI Homodimer. Periplasm.

KEGG Pathways
Map code Pathways E.C.

Compound table
Substrates Products Intermediates
KEGG-id C02582 C02582
E.C.
Compound Protein disulfide Protein disulfide
Type disulfide bond,peptide/protein disulfide bond,peptide/protein
ChEBI
PubChem
1eejA01 Unbound Unbound
1eejB01 Unbound Unbound
1g0tA01 Unbound Unbound
1g0tB01 Unbound Unbound
1jzdA01 Unbound Unbound
1jzdB01 Unbound Unbound
1jzoA01 Unbound Unbound
1jzoB01 Unbound Unbound
1tjdA01 Unbound Unbound
1eejA02 Unbound Unbound
1eejB02 Unbound Unbound
1g0tA02 Unbound Unbound
1g0tB02 Unbound Unbound
1jzdA02 Unbound Unbound
1jzdB02 Unbound Unbound
1jzoA02 Unbound Unbound
1jzoB02 Unbound Unbound
1tjdA02 Unbound Unbound

Reference for Active-site residues
resource references E.C.
literature [3], [4]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1eejA01
1eejB01
1g0tA01
1g0tB01
1jzdA01
1jzdB01
1jzoA01
1jzoB01
1tjdA01
1eejA02 CYS 98;CYS 101
1eejB02 CYS 98;CYS 101
1g0tA02 CYS 98; mutant C101S
1g0tB02 CYS 98; mutant C101S
1jzdA02 CYS 98; mutant C101S
1jzdB02 CYS 98; mutant C101S
1jzoA02 CYS 98; mutant C101S
1jzoB02 CYS 98; mutant C101S
1tjdA02 CYS 98;CYS 101

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[3]
Fig.8, p.15815
[4]
p.197-198
[7]
p.4780-4781
[8]
p.120-121
[9]
[11]
Fig.1

References
[1]
Resource
Comments CHARACTERIZATION.
Medline ID 94222048
PubMed ID 8168497
Journal EMBO J
Year 1994
Volume 13
Pages 2007-12
Authors Shevchik VE, Condemine G, Robert-Baudouy J
Title Characterization of DsbC, a periplasmic protein of Erwinia chrysanthemi and Escherichia coli with disulfide isomerase activity.
Related PDB
Related UniProtKB P21892
[2]
Resource
Comments CHARACTERIZATION, MUTAGENESIS, AND REVISION TO 219.
Medline ID 95226395
PubMed ID 7536035
Journal Biochemistry
Year 1995
Volume 34
Pages 5075-89
Authors Zapun A, Missiakas D, Raina S, Creighton TE
Title Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli.
Related PDB
Related UniProtKB P21892
[3]
Resource
Comments
Medline ID
PubMed ID 9398311
Journal Biochemistry
Year 1997
Volume 36
Pages 15810-6
Authors Chivers PT, Raines RT
Title General acid/base catalysis in the active site of Escherichia coli thioredoxin.
Related PDB
Related UniProtKB
[4]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
Medline ID 20165176
PubMed ID 10700276
Journal Nat Struct Biol
Year 2000
Volume 7
Pages 196-9
Authors McCarthy AA, Haebel PW, Torronen A, Rybin V, Baker EN, Metcalf P
Title Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli.
Related PDB 1eej
Related UniProtKB P21892
[5]
Resource
Comments
Medline ID
PubMed ID 11886218
Journal J Struct Biol
Year 2001
Volume 136
Pages 162-6
Authors Haebel PW, Wichman S, Goldstone D, Metcalf P
Title Crystallization and initial crystallographic analysis of the disulfide bond isomerase DsbC in complex with the alpha domain of the electron transporter DsbD.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 11493705
Journal Proc Natl Acad Sci U S A
Year 2001
Volume 98
Pages 9551-6
Authors Goldstone D, Haebel PW, Katzen F, Bader MW, Bardwell JC, Beckwith J, Metcalf P
Title DsbC activation by the N-terminal domain of DsbD.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 12234918
Journal EMBO J
Year 2002
Volume 21
Pages 4774-84
Authors Haebel PW, Goldstone D, Katzen F, Beckwith J, Metcalf P
Title The disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: crystal structure of the DsbC-DsbDalpha complex.
Related PDB 1g0t 1jzo 1jzd
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 12524212
Journal Annu Rev Biochem
Year 2003
Volume 72
Pages 111-35
Authors Kadokura H, Katzen F, Beckwith J
Title Protein disulfide bond formation in prokaryotes.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 15388920
Journal Acta Crystallogr D Biol Crystallogr
Year 2004
Volume 60
Pages 1747-52
Authors Banaszak K, Mechin I, Frost G, Rypniewski W
Title Structure of the reduced disulfide-bond isomerase DsbC from Escherichia coli.
Related PDB 1tjd
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 15057279
Journal EMBO J
Year 2004
Volume 23
Pages 1709-19
Authors Rozhkova A, Stirnimann CU, Frei P, Grauschopf U, Brunisholz R, Grutter MG, Capitani G, Glockshuber R
Title Structural basis and kinetics of inter- and intramolecular disulfide exchange in the redox catalyst DsbD.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 15546661
Journal Biochim Biophys Acta
Year 2004
Volume 1694
Pages 111-9
Authors Nakamoto H, Bardwell JC
Title Catalysis of disulfide bond formation and isomerization in the Escherichia coli periplasm.
Related PDB
Related UniProtKB

Comments
According to the literature [11], this enzyme catalyzes the following reaction.
(A) Electron transfer from the active site (Cys98/Cys101) to the disulfide bond of the misfolded substrate protein, producing correctly folded protein.
(B) Electron transfer from DsbD enzyme (Swissprot;P36655) to the disulfide bond of the active site, recovering the active site.

Created Updated
2005-06-14 2009-02-26