› 4ghc

X-ray diffraction
1.55Å resolution

Structure of Y257F variant of Homoprotocatechuate 2,3-Dioxygenase from B.fuscum at 1.55 Ang resolution

Released:
DOI: 10.2210/pdb4ghc/pdb
PDB entry 4ghc coloured by chain, front view.
PDB entry 4ghc coloured by chain, side view.
PDB entry 4ghc coloured by chain, top view.
Source organism: Brevibacterium fuscum
Primary publication:
Structural basis for the role of tyrosine 257 of homoprotocatechuate 2,3-dioxygenase in substrate and oxygen activation.
Kovaleva EG, Lipscomb JD
Biochemistry 51 8755-63 (2012)
PMID: 23066739

Function and Biology Details

Reaction catalysed: 
3,4-dihydroxyphenylacetate + O(2) = 2-hydroxy-5-carboxymethylmuconate semialdehyde
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-175045 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
VOC domain-containing protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 365 amino acids
Theoretical weight: 41.74 KDa
Source organism: Brevibacterium fuscum
Expression system: Escherichia coli
UniProt:
  • Canonical: Q45135 (Residues: 1-365; Coverage: 100%)
Sequence domains: Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand FE2 4 x FE2
Ligand CL 4 x CL
Ligand GOL 9 x GOL
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P21212
Unit cell:
a: 110.356Å b: 151.736Å c: 96.335Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.119 0.117 0.148
Expression system: Escherichia coli

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Citations

4 review citations

Oxygen activation by mononuclear nonheme iron dioxygenases involved in the degradation of aromatics.
Wang et al. (2017)
3 more

1 mention without citation

Structural basis for the role of tyrosine 257 of homoprotocatechuate 2,3-dioxygenase in substrate and oxygen activation.
Kovaleva et al. (2012)