› 1kek

X-ray diffraction
1.9Å resolution

Crystal Structure of the Free Radical Intermediate of Pyruvate:Ferredoxin Oxidoreductase

Released:
DOI: 10.2210/pdb1kek/pdb
PDB entry 1kek coloured by chain, front view.
PDB entry 1kek coloured by chain, side view.
PDB entry 1kek coloured by chain, top view.
Source organism: Desulfocurvibacter africanus
Primary publication:
Crystal structure of the free radical intermediate of pyruvate:ferredoxin oxidoreductase.
Chabrière E, Vernède X, Guigliarelli B, Charon MH, Hatchikian EC, Fontecilla-Camps JC
Science 294 2559-63 (2001)
PMID: 11752578

Function and Biology Details

Reaction catalysed: 
Pyruvate + CoA + 2 oxidized ferredoxin = acetyl-CoA + CO(2) + 2 reduced ferredoxin + 2 H(+)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161130 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:

Ligands and Environments


Cofactor: Ligand HTL 2 x HTL
4 bound ligands:
Ligand MG 2 x MG
Ligand CA 2 x CA
Ligand SF4 6 x SF4
Ligand CO2 2 x CO2
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-3
Spacegroup: P212121
Unit cell:
a: 86.11Å b: 145.76Å c: 210.26Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.178 0.178 0.227

Quick links

Citations

10 review citations

Acetogenesis and the Wood-Ljungdahl pathway of CO(2) fixation.
Ragsdale et al. (2008)
9 more

8 mentions without citation

Enzymology of the wood-Ljungdahl pathway of acetogenesis.
Ragsdale SW. (2008)
7 more