› 2w23

X-ray diffraction
1.94Å resolution

Structure of mutant W169Y of Pleurotus eryngii versatile peroxidase (VP)

Released:
DOI: 10.2210/pdb2w23/pdb
PDB entry 2w23 coloured by chain, front view.
PDB entry 2w23 coloured by chain, side view.
PDB entry 2w23 coloured by chain, top view.
Source organism: Pleurotus eryngii
Primary publication:
Protein radicals in fungal versatile peroxidase: catalytic tryptophan radical in both compound I and compound II and studies on W164Y, W164H, and W164S variants.
Ruiz-Dueñas FJ, Pogni R, Morales M, Giansanti S, Mate MJ, Romero A, Martínez MJ, Basosi R, Martínez AT
J Biol Chem 284 7986-94 (2009)
PMID: 19158088

Function and Biology Details

Reaction catalysed: 
1-(4-hydroxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H(2)O(2) = 4-hydroxy-3-methoxybenzaldehyde + 2-methoxyphenol + glycolaldehyde + H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-131734 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Versatile peroxidase VPL2 Chain: A
Molecule details ›
Chain: A
Length: 316 amino acids
Theoretical weight: 33.22 KDa
Source organism: Pleurotus eryngii
Expression system: Escherichia coli
UniProt:
  • Canonical: O94753 (Residues: 31-346; Coverage: 93%)
Gene name: vpl2
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand HEM 1 x HEM
3 bound ligands:
Ligand CA 2 x CA
Ligand SO4 1 x SO4
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: I41
Unit cell:
a: 96.74Å b: 96.74Å c: 98.19Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.144 0.142 0.175
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Heme enzyme structure and function.
Poulos TL. (2014)
4 more

2 mentions without citation

Two oxidation sites for low redox potential substrates: a directed mutagenesis, kinetic, and crystallographic study on Pleurotus eryngii versatile peroxidase.
Morales et al. (2012)
1 more