› 2c42

X-ray diffraction
1.78Å resolution

Crystal Structure Of Pyruvate-Ferredoxin Oxidoreductase From Desulfovibrio africanus

Released:
DOI: 10.2210/pdb2c42/pdb
PDB entry 2c42 coloured by chain, front view.
PDB entry 2c42 coloured by chain, side view.
PDB entry 2c42 coloured by chain, top view.
Source organism: Desulfocurvibacter africanus
Primary publication:
Flexibility of thiamine diphosphate revealed by kinetic crystallographic studies of the reaction of pyruvate-ferredoxin oxidoreductase with pyruvate.
Cavazza C, Contreras-Martel C, Pieulle L, Chabrière E, Hatchikian EC, Fontecilla-Camps JC
Structure 14 217-24 (2006)
PMID: 16472741

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 TPP 2 x TPP
4 bound ligands:
Ligand SF4 6 x SF4
Ligand PYR 2 x PYR
Ligand MG 2 x MG
Ligand CA 2 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P212121
Unit cell:
a: 86.304Å b: 145.981Å c: 211.607Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.195 0.219

Quick links

Citations

4 review citations

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

7 mentions without citation

A structural phylogeny for understanding 2-oxoacid oxidoreductase function.
Gibson et al. (2016)
6 more