› 1zof

X-ray diffraction
2.95Å resolution

Crystal structure of alkyl hydroperoxide-reductase (AhpC) from Helicobacter Pylori

Released:
DOI: 10.2210/pdb1zof/pdb
PDB entry 1zof coloured by chain, front view.
PDB entry 1zof coloured by chain, side view.
PDB entry 1zof coloured by chain, top view.
Source organism: Helicobacter pylori
Primary publication:
Crystal structure of alkyl hydroperoxide-reductase (AhpC) from Helicobacter pylori.
Papinutto E, Windle HJ, Cendron L, Battistutta R, Kelleher D, Zanotti G
Biochim Biophys Acta 1753 240-6 (2005)
PMID: 16213196

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo decamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157574 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alkyl hydroperoxide reductase C Chains: A, B, C, D, E, F, G, H, I, J
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J
Length: 198 amino acids
Theoretical weight: 22.28 KDa
Source organism: Helicobacter pylori
Expression system: Escherichia coli
UniProt:
  • Canonical: P56876 (Residues: 1-198; Coverage: 100%)
Gene names: ahpC, jhp_1471, tsaA
Sequence domains:
Structure domains: Glutaredoxin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: C2
Unit cell:
a: 193.86Å b: 138.42Å c: 127.54Å
α: 90° β: 125.7° γ: 90°
R-values:
R R work R free
0.236 0.236 0.26
Expression system: Escherichia coli

Quick links

Citations

6 review citations

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

8 mentions without citation

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