› 3bg5

X-ray diffraction
2.8Å resolution

Crystal Structure of Staphylococcus Aureus Pyruvate Carboxylase

Released:
DOI: 10.2210/pdb3bg5/pdb
PDB entry 3bg5 coloured by chain, front view.
PDB entry 3bg5 coloured by chain, side view.
PDB entry 3bg5 coloured by chain, top view.
Source organism: Staphylococcus aureus
Primary publication:
Crystal structures of human and Staphylococcus aureus pyruvate carboxylase and molecular insights into the carboxyltransfer reaction.
Xiang S, Tong L
Nat Struct Mol Biol 15 295-302 (2008)
PMID: 18297087

Function and Biology Details

Reaction catalysed: 
ATP + pyruvate + HCO(3)(-) = ADP + phosphate + oxaloacetate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
homo tetramer
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-101945 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:

Ligands and Environments


Cofactor: Ligand BTI 4 x BTI
3 bound ligands:
Ligand MN 4 x MN
Ligand PYR 4 x PYR
Ligand ATP 2 x ATP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: P21
Unit cell:
a: 96.428Å b: 256.083Å c: 126.01Å
α: 90° β: 109.47° γ: 90°
R-values:
R R work R free
0.217 0.215 0.268
Expression system: Escherichia coli

Quick links

Citations

11 review citations

Regulation of pyruvate metabolism and human disease.
Gray et al. (2014)
10 more

12 mentions without citation

Insight into the carboxyl transferase domain mechanism of pyruvate carboxylase from Rhizobium etli.
Zeczycki et al. (2009)
11 more