› 2nvl

X-ray diffraction
2.36Å resolution

Crystal structure of archaeal peroxiredoxin, thioredoxin peroxidase from Aeropyrum pernix K1 (sulfonic acid form)

Released:
DOI: 10.2210/pdb2nvl/pdb
PDB entry 2nvl coloured by chain, front view.
PDB entry 2nvl coloured by chain, side view.
PDB entry 2nvl coloured by chain, top view.
Source organism: Aeropyrum pernix K1
Primary publication:
Oxidation of archaeal peroxiredoxin involves a hypervalent sulfur intermediate.
Nakamura T, Yamamoto T, Abe M, Matsumura H, Hagihara Y, Goto T, Yamaguchi T, Inoue T
Proc Natl Acad Sci U S A 105 6238-42 (2008)
PMID: 18436649

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

Assembly composition:
homo decamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195428 (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: 250 amino acids
Theoretical weight: 28.78 KDa
Source organism: Aeropyrum pernix K1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Y9L0 (Residues: 1-250; Coverage: 100%)
Gene name: APE_2278
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
1 modified residue:
Ligand OCS 10 x OCS

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P1
Unit cell:
a: 76.319Å b: 102.962Å c: 104.3Å
α: 105.65° β: 105.26° γ: 92.69°
R-values:
R R work R free
0.169 0.166 0.219
Expression system: Escherichia coli

Quick links

Citations

13 review citations

Cysteine-mediated redox signaling: chemistry, biology, and tools for discovery.
Paulsen et al. (2013)
12 more

6 mentions without citation

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