› 2hj3

X-ray diffraction
2.5Å resolution

Structure of the Arabidopsis Thaliana Erv1 Thiol Oxidase

Released:
DOI: 10.2210/pdb2hj3/pdb
PDB entry 2hj3 coloured by chain, front view.
PDB entry 2hj3 coloured by chain, side view.
PDB entry 2hj3 coloured by chain, top view.
Source organism: Arabidopsis thaliana
Primary publication:
Gain of function in an ERV/ALR sulfhydryl oxidase by molecular engineering of the shuttle disulfide.
Vitu E, Bentzur M, Lisowsky T, Kaiser CA, Fass D
J Mol Biol 362 89-101 (2006)
PMID: 16893552

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 analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-184592 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
FAD-linked sulfhydryl oxidase ERV1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 125 amino acids
Theoretical weight: 14.4 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8GXX0 (Residues: 71-191; Coverage: 63%)
Gene names: At1g49880, ERV1, F10F5.3
Sequence domains: Erv1 / Alr family
Structure domains: ERV/ALR sulfhydryl oxidase domain

Ligands and Environments


Cofactor: Ligand FAD 2 x FAD
1 bound ligand:
Ligand SO4 12 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU, ESRF BEAMLINE BM14
Spacegroup: P6522
Unit cell:
a: 82.84Å b: 82.84Å c: 160.813Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.228 0.228 0.267
Expression system: Escherichia coli

Quick links

Citations

21 review citations

Flavoenzymes.
Joosten et al. (2007)
20 more

2 mentions without citation

Deciphering structural and functional roles of individual disulfide bonds of the mitochondrial sulfhydryl oxidase Erv1p.
Ang et al. (2009)
1 more