› 2hzf

X-ray diffraction
1.8Å resolution

Crystal structures of a poxviral glutaredoxin in the oxidized and reduced states show redox-correlated structural changes

Released:
DOI: 10.2210/pdb2hzf/pdb
PDB entry 2hzf coloured by chain, front view.
PDB entry 2hzf coloured by chain, side view.
PDB entry 2hzf coloured by chain, top view.
Source organism: Ectromelia virus Moscow
Primary publication:
Crystal structures of a poxviral glutaredoxin in the oxidized and reduced states show redox-correlated structural changes.
Bacik JP, Hazes B
J Mol Biol 365 1545-58 (2007)
PMID: 17137595

Function and Biology Details

Reaction catalysed: 
2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-185002 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutaredoxin-1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 114 amino acids
Theoretical weight: 13.16 KDa
Source organism: Ectromelia virus Moscow
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8JLF5 (Residues: 1-108; Coverage: 100%)
Gene names: EVM053, OPG075
Sequence domains: Glutaredoxin
Structure domains: Glutaredoxin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: C2221
Unit cell:
a: 61.976Å b: 67.573Å c: 108.553Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.18 0.219
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Glutathione catalysis and the reaction mechanisms of glutathione-dependent enzymes.
Deponte M. (2013)
1 more

3 mentions without citation

Poxvirus proteomics and virus-host protein interactions.
Van Vliet et al. (2009)
2 more