› 3gkk

X-ray diffraction
1.83Å resolution

Insights into the Alkyl Peroxide Reduction Activity of Xanthomonas campestris Bacterioferritin Comigratory Protein from the Trapped Intermediate/Ligand Complex Structures

Released:
DOI: 10.2210/pdb3gkk/pdb
PDB entry 3gkk coloured by chain, front view.
PDB entry 3gkk coloured by chain, side view.
PDB entry 3gkk coloured by chain, top view.
Source organism: Xanthomonas campestris pv. campestris
Primary publication:
Insights into the alkyl peroxide reduction pathway of Xanthomonas campestris bacterioferritin comigratory protein from the trapped intermediate-ligand complex structures.
Liao SJ, Yang CY, Chin KH, Wang AH, Chou SH
J Mol Biol 390 951-66 (2009)
PMID: 19477183

Function and Biology Details

Reaction catalysed: 
Thioredoxin + ROOH = thioredoxin disulfide + H(2)O + ROH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-185726 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peroxiredoxin Bcp Chain: A
Molecule details ›
Chain: A
Length: 163 amino acids
Theoretical weight: 17.57 KDa
Source organism: Xanthomonas campestris pv. campestris
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8P9V9 (Residues: 1-160; Coverage: 100%)
Gene names: XCC1738, bcp
Sequence domains: AhpC/TSA family
Structure domains: Glutaredoxin

Ligands and Environments

1 bound ligand:
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13C1, SPRING-8 BEAMLINE BL12B2
Spacegroup: P21
Unit cell:
a: 34.835Å b: 54.646Å c: 36.645Å
α: 90° β: 108.23° γ: 90°
R-values:
R R work R free
0.179 0.179 0.228
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Why do bacteria use so many enzymes to scavenge hydrogen peroxide?
Mishra et al. (2012)
2 more

5 mentions without citation

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