› 1jqn

X-ray diffraction
2.35Å resolution

Crystal structure of E.coli phosphoenolpyruvate carboxylase in complex with Mn2+ and DCDP

Released:
DOI: 10.2210/pdb1jqn/pdb
PDB entry 1jqn coloured by chain, front view.
PDB entry 1jqn coloured by chain, side view.
PDB entry 1jqn coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structures of C4 form maize and quaternary complex of E. coli phosphoenolpyruvate carboxylases.
Matsumura H, Xie Y, Shirakata S, Inoue T, Yoshinaga T, Ueno Y, Izui K, Kai Y
Structure 10 1721-30 (2002)
PMID: 12467579

Function and Biology Details

Reaction catalysed: 
Phosphate + oxaloacetate = H(2)O + phosphoenolpyruvate + HCO(3)(-)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133647 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoenolpyruvate carboxylase Chain: A
Molecule details ›
Chain: A
Length: 883 amino acids
Theoretical weight: 99.18 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P00864 (Residues: 1-883; Coverage: 100%)
Gene names: JW3928, b3956, glu, ppc
Sequence domains: Phosphoenolpyruvate carboxylase

Ligands and Environments

3 bound ligands:
Ligand MN 1 x MN
Ligand ASP 1 x ASP
Ligand DCO 1 x DCO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-18B
Spacegroup: I222
Unit cell:
a: 117.95Å b: 249.06Å c: 83.12Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.195 0.231
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Phosphoenolpyruvate carboxylase: a new era of structural biology.
Izui et al. (2004)
6 more

9 mentions without citation

Enzymatic Conversion of CO2: From Natural to Artificial Utilization.
Bierbaumer et al. (2023)
8 more