› 1jpe

X-ray diffraction
1.9Å resolution

Crystal structure of DsbD-alpha; the N-terminal domain of DsbD

Released:
DOI: 10.2210/pdb1jpe/pdb
PDB entry 1jpe coloured by chain, front view.
PDB entry 1jpe coloured by chain, side view.
PDB entry 1jpe coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
The disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: crystal structure of the DsbC-DsbDalpha complex.
Haebel PW, Goldstone D, Katzen F, Beckwith J, Metcalf P
EMBO J 21 4774-84 (2002)
PMID: 12234918

Function and Biology Details

Reaction catalysed: 
Protein dithiol + NAD(P)(+) = protein disulfide + NAD(P)H
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153206 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thiol:disulfide interchange protein DsbD Chain: A
Molecule details ›
Chain: A
Length: 151 amino acids
Theoretical weight: 17.09 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P36655 (Residues: 19-151; Coverage: 24%)
Gene names: JW5734, b4136, cutA2, cycZ, dipZ, dsbD
Sequence domains: Thiol:disulfide interchange protein DsbD, N-terminal
Structure domains: Thiol:disulfide interchange protein DsbD, N-terminal domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: C2221
Unit cell:
a: 53.082Å b: 54.603Å c: 102.478Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.239 0.216 0.254
Expression system: Escherichia coli

Quick links

Citations

27 review citations

Protein disulfide bond formation in prokaryotes.
Kadokura et al. (2003)
26 more

14 mentions without citation

Disulfide bond formation in the bacterial periplasm: major achievements and challenges ahead.
Denoncin et al. (2013)
13 more