› 1jr8

X-ray diffraction
1.5Å resolution

Crystal Structure of Erv2p

Released:
DOI: 10.2210/pdb1jr8/pdb
PDB entry 1jr8 coloured by chain, front view.
PDB entry 1jr8 coloured by chain, side view.
PDB entry 1jr8 coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p.
Gross E, Sevier CS, Vala A, Kaiser CA, Fass D
Nat Struct Biol 9 61-7 (2002)
PMID: 11740506

Function and Biology Details

Reaction catalysed: 
2 R'C(R)SH + O(2) = R'C(R)S-S(R)CR' + H(2)O(2)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171328 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
FAD-linked sulfhydryl oxidase ERV2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 117 amino acids
Theoretical weight: 13.52 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q12284 (Residues: 71-187; Coverage: 60%)
Gene names: ERV2, YP3085.03C, YPR037C
Sequence domains: Erv1 / Alr family
Structure domains: ERV/ALR sulfhydryl oxidase domain

Ligands and Environments


Cofactor: Ligand FAD 2 x FAD
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300, ESRF BEAMLINE ID14-4
Spacegroup: P21
Unit cell:
a: 47.64Å b: 45.15Å c: 53.84Å
α: 90° β: 100.15° γ: 90°
R-values:
R R work R free
0.208 0.208 0.233
Expression system: Escherichia coli

Quick links

Citations

40 review citations

Importing mitochondrial proteins: machineries and mechanisms.
Chacinska et al. (2009)
39 more

14 mentions without citation

Oxidative protein folding and the Quiescin-sulfhydryl oxidase family of flavoproteins.
Kodali et al. (2010)
13 more