› 1ti1

X-ray diffraction
2.6Å resolution

crystal structure of a mutant DsbA

Released:
DOI: 10.2210/pdb1ti1/pdb
PDB 1ti1 coloured by chain and viewed from the front.
PDB 1ti1 coloured by chain and viewed from the side.
PDB 1ti1 coloured by chain and viewed from the top.
Source organism: Escherichia coli O157:H7
Primary publication:
Intriguing conformation changes associated with the trans/cis isomerization of a prolyl residue in the active site of the DsbA C33A mutant.
Ondo-Mbele E, Vivès C, Koné A, Serre L
J Mol Biol 347 555-63 (2005)
PMID: 15755450

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thiol:disulfide interchange protein DsbA Chain: A
Molecule details ›
Chain: A
Length: 189 amino acids
Theoretical weight: 21.12 KDa
Source organism: Escherichia coli O157:H7
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

Ligands and Environments

1 bound ligand:
Ligand D12 1 x D12
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P62
Unit cell:
a: 57.16Å b: 57.16Å c: 109.8Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.247 0.247 0.279
Expression system: Escherichia coli

Quick links

Citations

1 review citation

The name's bond......disulfide bond.
Heras et al. (2007)
7 other articles

1 mention without citation

The Redox State Regulates the Conformation of Rv2466c to Activate the Antitubercular Prodrug TP053.
Albesa-Jové et al. (2015)