› 1xvw

X-ray diffraction
1.9Å resolution

Crystal Structure of AhpE from Mycobacterium tuberculosis, a 1-Cys peroxiredoxin

Released:
DOI: 10.2210/pdb1xvw/pdb
PDB entry 1xvw coloured by chain, front view.
PDB entry 1xvw coloured by chain, side view.
PDB entry 1xvw coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
Crystal Structure of AhpE from Mycobacterium tuberculosis, a 1-Cys peroxiredoxin.
Li S, Peterson NA, Kim MY, Kim CY, Hung LW, Yu M, Lekin T, Segelke BW, Lott JS, Baker EN
J Mol Biol 346 1035-46 (2005)
PMID: 15701515

Function and Biology Details

Reaction catalysed: 
Mycoredoxin + ROOH = mycoredoxin disulfide + H(2)O + ROH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161624 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alkyl hydroperoxide reductase E Chains: A, B
Molecule details ›
Chains: A, B
Length: 160 amino acids
Theoretical weight: 17.61 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P9WIE3 (Residues: 1-153; Coverage: 100%)
Gene names: MTCY427.19c, Rv2238c, ahpE
Sequence domains: AhpC/TSA family
Structure domains: Glutaredoxin

Ligands and Environments

No bound ligands
1 modified residue:
Ligand CSO 2 x CSO

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: I4
Unit cell:
a: 147.994Å b: 147.994Å c: 33.711Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.18 0.21
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

9 review citations

The oligomeric conformation of peroxiredoxins links redox state to function.
Barranco-Medina et al. (2009)
8 more

4 mentions without citation

Structure-based insights into the catalytic power and conformational dexterity of peroxiredoxins.
Hall et al. (2011)
3 more