› 4tky

X-ray diffraction
2.5Å resolution

The complex structure of E. coli DsbA bound to a peptide at the DsbA/DsbB interface

Released:
DOI: 10.2210/pdb4tky/pdb
PDB entry 4tky coloured by chain, front view.
PDB entry 4tky coloured by chain, side view.
PDB entry 4tky coloured by chain, top view.
Source organisms:
Primary publication:
Peptide inhibitors of the Escherichia coli DsbA oxidative machinery essential for bacterial virulence.
Duprez W, Premkumar L, Halili MA, Lindahl F, Reid RC, Fairlie DP, Martin JL
J Med Chem 58 577-87 (2015)
PMID: 25470204

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142451 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Thiol:disulfide interchange protein DsbA Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 191 amino acids
Theoretical weight: 21.32 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AEG4 (Residues: 20-208; Coverage: 100%)
Gene names: JW3832, b3860, dsbA, dsf, ppfA
Sequence domains: DSBA-like thioredoxin domain
Structure domains: Glutaredoxin
PRO-PHE-ALA-THR-CYS-ASP-SER Chains: E, F, G, H
Molecule details ›
Chains: E, F, G, H
Length: 7 amino acids
Theoretical weight: 740 Da
Source organism: Escherichia coli
Expression system: Not provided

Ligands and Environments

2 bound ligands:
Ligand ACE 4 x ACE
Ligand NH2 4 x NH2
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX1
Spacegroup: P1
Unit cell:
a: 59.959Å b: 62.533Å c: 67.26Å
α: 99.55° β: 103.8° γ: 114°
R-values:
R R work R free
0.179 0.176 0.237
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

8 review citations

Disulfide bond formation in prokaryotes.
Landeta et al. (2018)
7 more

4 mentions without citation

Targeting Bacterial Dsb Proteins for the Development of Anti-Virulence Agents.
Smith et al. (2016)
3 more