› 1x0r

X-ray diffraction
2Å resolution

Thioredoxin Peroxidase from Aeropyrum pernix K1

Released:
DOI: 10.2210/pdb1x0r/pdb
PDB entry 1x0r coloured by chain, front view.
PDB entry 1x0r coloured by chain, side view.
PDB entry 1x0r coloured by chain, top view.
Source organism: Aeropyrum pernix K1
Primary publication:
Crystal structure of thioredoxin peroxidase from aerobic hyperthermophilic archaeon Aeropyrum pernix K1.
Nakamura T, Yamamoto T, Inoue T, Matsumura H, Kobayashi A, Hagihara Y, Uegaki K, Ataka M, Kai Y, Ishikawa K
Proteins 62 822-6 (2006)
PMID: 16342268

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo decamer
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195430 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peroxiredoxin 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: 249 amino acids
Theoretical weight: 28.78 KDa
Source organism: Aeropyrum pernix K1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Y9L0 (Residues: 2-250; Coverage: 100%)
Gene name: APE_2278
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand EDO 128 x EDO
1 modified residue:
Ligand MSE 40 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL38B1
Spacegroup: P1
Unit cell:
a: 75.633Å b: 101.792Å c: 102.886Å
α: 105.37° β: 105.28° γ: 93.32°
R-values:
R R work R free
0.164 0.164 0.171
Expression system: Escherichia coli

Quick links

Citations

3 review citations

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

1 mention without citation

Structural evidence that peroxiredoxin catalytic power is based on transition-state stabilization.
Hall et al. (2010)