› 3odm

X-ray diffraction
2.95Å resolution

Archaeal-type phosphoenolpyruvate carboxylase

Released:
DOI: 10.2210/pdb3odm/pdb
PDB entry 3odm coloured by chain, front view.
PDB entry 3odm coloured by chain, side view.
PDB entry 3odm coloured by chain, top view.
Source organism: Clostridium perfringens
Primary publication:
Structure of an archaeal-type phosphoenolpyruvate carboxylase sensitive to inhibition by aspartate.
Dharmarajan L, Kraszewski JL, Mukhopadhyay B, Dunten PW
Proteins 79 1820-9 (2011)
PMID: 21491491

Function and Biology Details

Reaction catalysed: 
Phosphate + oxaloacetate = H(2)O + phosphoenolpyruvate + HCO(3)(-)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
homo tetramer
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-186898 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoenolpyruvate carboxylase Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 560 amino acids
Theoretical weight: 63.35 KDa
Source organism: Clostridium perfringens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8XLE8 (Residues: 1-537; Coverage: 100%)
Gene names: CPE1094, ppcA
Sequence domains: Phosphoenolpyruvate carboxylase

Ligands and Environments

2 bound ligands:
Ligand AUC 36 x AUC
Ligand MLI 5 x MLI
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: P212121
Unit cell:
a: 121.42Å b: 161.58Å c: 279.98Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.178 0.178 0.223
Expression system: Escherichia coli

Quick links

Citations

4 citation in other articles

Greater efficiency of photosynthetic carbon fixation due to single amino-acid substitution.
Paulus et al. (2013)
3 more

2 mentions without citation

Phosphoenolpyruvate carboxylase identified as a key enzyme in erythrocytic Plasmodium falciparum carbon metabolism.
Storm et al. (2014)
1 more