› 1pt8

X-ray diffraction
2.2Å resolution

Crystal structure of the yfdW gene product of E. coli, in complex with oxalate and acetyl-CoA

Released:
DOI: 10.2210/pdb1pt8/pdb
PDB entry 1pt8 coloured by chain, front view.
PDB entry 1pt8 coloured by chain, side view.
PDB entry 1pt8 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
The crystal structure of the Escherichia coli YfdW gene product reveals a new fold of two interlaced rings identifying a wide family of CoA transferases.
Gruez A, Roig-Zamboni V, Valencia C, Campanacci V, Cambillau C
J Biol Chem 278 34582-6 (2003)
PMID: 12844490

Function and Biology Details

Reaction catalysed: 
Formyl-CoA + oxalate = formate + oxalyl-CoA
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159681 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Formyl-CoA:oxalate CoA-transferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 437 amino acids
Theoretical weight: 48.41 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P69902 (Residues: 1-416; Coverage: 100%)
Gene names: JW2371, b2374, frc, yfdW
Sequence domains: CoA-transferase family III
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand OXL 2 x OXL
Ligand ACO 2 x ACO
Ligand GOL 5 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P62
Unit cell:
a: 146.786Å b: 146.786Å c: 129.905Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.182 0.181 0.204
Expression system: Escherichia coli

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Citations

3 review citations

The enzymes of oxalate metabolism: unexpected structures and mechanisms.
Svedruzić et al. (2005)
2 more