› 1p5h

X-ray diffraction
2.2Å resolution

Crystal structure of Formyl-CoA Transferase (apoenzyme) from Oxalobacter formigenes

Released:
DOI: 10.2210/pdb1p5h/pdb
PDB entry 1p5h coloured by chain, front view.
PDB entry 1p5h coloured by chain, side view.
PDB entry 1p5h coloured by chain, top view.
Source organism: Oxalobacter formigenes
Primary publication:
Formyl-CoA transferase encloses the CoA binding site at the interface of an interlocked dimer.
Ricagno S, Jonsson S, Richards N, Lindqvist Y
EMBO J 22 3210-9 (2003)
PMID: 12839984

Function and Biology Details

Reaction catalysed: 
Formyl-CoA + oxalate = formate + oxalyl-CoA
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-126525 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Formyl-CoA:oxalate CoA-transferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 428 amino acids
Theoretical weight: 47.38 KDa
Source organism: Oxalobacter formigenes
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O06644 (Residues: 1-428; Coverage: 100%)
Gene name: frc
Sequence domains: CoA-transferase family III
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1, EMBL/DESY, HAMBURG BEAMLINE BW7A
Spacegroup: I4
Unit cell:
a: 151.44Å b: 151.44Å c: 99.49Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.173 0.171 0.209
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

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

4 mentions without citation

Formyl-CoA transferase encloses the CoA binding site at the interface of an interlocked dimer.
Ricagno et al. (2003)
3 more