› 3i43

X-ray diffraction
2.8Å resolution

Escherichia coli Thiol peroxidase (Tpx) wild type disulfide form

Released:
DOI: 10.2210/pdb3i43/pdb
PDB entry 3i43 coloured by chain, front view.
PDB entry 3i43 coloured by chain, side view.
PDB entry 3i43 coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Structural changes common to catalysis in the Tpx peroxiredoxin subfamily.
Hall A, Sankaran B, Poole LB, Karplus PA
J Mol Biol 393 867-81 (2009)
PMID: 19699750

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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141668 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thiol peroxidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 167 amino acids
Theoretical weight: 17.72 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A862 (Residues: 2-168; Coverage: 99%)
Gene names: JW1317, b1324, tpx, yzzJ
Sequence domains: Redoxin
Structure domains: Glutaredoxin

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P212121
Unit cell:
a: 38.83Å b: 64Å c: 137.95Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.198 0.219
Expression system: Escherichia coli

Quick links

Citations

9 review citations

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

4 mentions without citation

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