› 4k6x

X-ray diffraction
1.97Å resolution

Crystal structure of disulfide oxidoreductase from Mycobacterium tuberculosis

Released:
DOI: 10.2210/pdb4k6x/pdb
PDB entry 4k6x coloured by chain, front view.
PDB entry 4k6x coloured by chain, side view.
PDB entry 4k6x coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
Rv2969c, essential for optimal growth in Mycobacterium tuberculosis, is a DsbA-like enzyme that interacts with VKOR-derived peptides and has atypical features of DsbA-like disulfide oxidases.
Premkumar L, Heras B, Duprez W, Walden P, Halili M, Kurth F, Fairlie DP, Martin JL
Acta Crystallogr D Biol Crystallogr 69 1981-94 (2013)
PMID: 24100317

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-128476 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thioredoxin-like fold domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 213 amino acids
Theoretical weight: 22.28 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli
UniProt:
  • Canonical: O33272 (Residues: 46-255; Coverage: 82%)
Gene name: Rv2969c
Sequence domains: Thioredoxin
Structure domains: Glutaredoxin

Ligands and Environments

2 bound ligands:
Ligand EPE 1 x EPE
Ligand DIO 1 x DIO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: I4122
Unit cell:
a: 92.05Å b: 92.05Å c: 232.756Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.151 0.148 0.195
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Disulfide-Bond-Forming Pathways in Gram-Positive Bacteria.
Reardon-Robinson et al. (2015)
5 more

5 mentions without citation

Rv2969c, essential for optimal growth in Mycobacterium tuberculosis, is a DsbA-like enzyme that interacts with VKOR-derived peptides and has atypical features of DsbA-like disulfide oxidases.
Premkumar et al. (2013)
4 more