› 1qb4

X-ray diffraction
2.6Å resolution

CRYSTAL STRUCTURE OF MN(2+)-BOUND PHOSPHOENOLPYRUVATE CARBOXYLASE

Released:
DOI: 10.2210/pdb1qb4/pdb
PDB entry 1qb4 coloured by chain, front view.
PDB entry 1qb4 coloured by chain, side view.
PDB entry 1qb4 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Plausible phosphoenolpyruvate binding site revealed by 2.6 A structure of Mn2+-bound phosphoenolpyruvate carboxylase from Escherichia coli.
Matsumura H, Terada M, Shirakata S, Inoue T, Yoshinaga T, Izui K, Kai Y
FEBS Lett 458 93-6 (1999)
PMID: 10481043

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

2 bound ligands:
Ligand MN 1 x MN
Ligand ASP 1 x ASP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-18B
Spacegroup: I222
Unit cell:
a: 117.75Å b: 248.41Å c: 83.47Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.221 0.223 0.261
Expression system: Escherichia coli

Quick links

Citations

6 review citations

The PEP-pyruvate-oxaloacetate node as the switch point for carbon flux distribution in bacteria.
Sauer et al. (2005)
5 more

8 mentions without citation

Identification and functional verification of archaeal-type phosphoenolpyruvate carboxylase, a missing link in archaeal central carbohydrate metabolism.
Ettema et al. (2004)
7 more