› 4dsr

X-ray diffraction
2.91Å resolution

Crystal structure of peroxiredoxin Ahp1 from Saccharomyces cerevisiae in reduced form

Released:
DOI: 10.2210/pdb4dsr/pdb
PDB entry 4dsr coloured by chain, front view.
PDB entry 4dsr coloured by chain, side view.
PDB entry 4dsr coloured by chain, top view.
Source organism: Saccharomyces cerevisiae S288C
Primary publication:
Structural snapshots of yeast alkyl hydroperoxide reductase Ahp1 peroxiredoxin reveal a novel two-cysteine mechanism of electron transfer to eliminate reactive oxygen species.
Lian FM, Yu J, Ma XX, Yu XJ, Chen Y, Zhou CZ
J Biol Chem 287 17077-17087 (2012)
PMID: 22474296

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-153531 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peroxiredoxin AHP1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 184 amino acids
Theoretical weight: 20.15 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: P38013 (Residues: 1-176; Coverage: 100%)
Gene names: AHP1, L2916, L9354.5, YLR109W
Sequence domains: Redoxin
Structure domains: Glutaredoxin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: R3
Unit cell:
a: 154.463Å b: 154.463Å c: 90.966Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.241 0.239 0.274
Expression system: Escherichia coli

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Citations

4 review citations

Peroxiredoxins: guardians against oxidative stress and modulators of peroxide signaling.
Perkins et al. (2015)
3 more

6 mentions without citation

Structural snapshots of yeast alkyl hydroperoxide reductase Ahp1 peroxiredoxin reveal a novel two-cysteine mechanism of electron transfer to eliminate reactive oxygen species.
Lian et al. (2012)
5 more