› 2pg8

X-ray diffraction
3Å resolution

Crystal structure of R254K mutanat of DpgC with bound substrate analog

Released:
DOI: 10.2210/pdb2pg8/pdb
PDB entry 2pg8 coloured by chain, front view.
PDB entry 2pg8 coloured by chain, side view.
PDB entry 2pg8 coloured by chain, top view.
Source organism: Streptomyces toyocaensis
Primary publication:
Substrate recognition and catalysis by the cofactor-independent dioxygenase DpgC.
Fielding EN, Widboom PF, Bruner SD
Biochemistry 46 13994-4000 (2007)
PMID: 18004875

Function and Biology Details

Reaction catalysed: 
(3,5-dihydroxyphenyl)acetyl-CoA + O(2) = 2-(3,5-dihydroxyphenyl)-2-oxoacetate + CoA
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
homo hexamer
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-185150 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
(3,5-dihydroxyphenyl)acetyl-CoA 1,2-dioxygenase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 417 amino acids
Theoretical weight: 45.99 KDa
Source organism: Streptomyces toyocaensis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8KLK7 (Residues: 10-426; Coverage: 95%)
Gene name: BU52_01220
Sequence domains: Enoyl-CoA hydratase/isomerase
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand YE1 3 x YE1
Ligand OXY 2 x OXY
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: P21212
Unit cell:
a: 139.054Å b: 155.309Å c: 169.208Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.331 0.331 0.367
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Total biosynthesis: in vitro reconstitution of polyketide and nonribosomal peptide pathways.
Sattely et al. (2008)
5 more

1 mention without citation

Structural and biophysical characterization of BoxC from Burkholderia xenovorans LB400: a novel ring-cleaving enzyme in the crotonase superfamily.
Bains et al. (2009)