› 2dzd

X-ray diffraction
2.4Å resolution

Crystal structure of the biotin carboxylase domain of pyruvate carboxylase

Released:
DOI: 10.2210/pdb2dzd/pdb
PDB entry 2dzd coloured by chain, front view.
PDB entry 2dzd coloured by chain, side view.
PDB entry 2dzd coloured by chain, top view.
Source organism: Geobacillus thermodenitrificans
Primary publication:
Structure of the biotin carboxylase domain of pyruvate carboxylase from Bacillus thermodenitrificans.
Kondo S, Nakajima Y, Sugio S, Sueda S, Islam MN, Kondo H
Acta Crystallogr D Biol Crystallogr 63 885-90 (2007)
PMID: 17642515

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170276 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pyruvate carboxylase Chains: A, B
Molecule details ›
Chains: A, B
Length: 461 amino acids
Theoretical weight: 51.4 KDa
Source organism: Geobacillus thermodenitrificans
Expression system: Escherichia coli
UniProt:
  • Canonical: Q05FZ3 (Residues: 1-461; Coverage: 100%)
Gene name: pycA
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL24XU
Spacegroup: P212121
Unit cell:
a: 79.609Å b: 115.987Å c: 115.729Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.232 0.232 0.29
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Structure, function and selective inhibition of bacterial acetyl-coa carboxylase.
Polyak et al. (2012)
4 other articles

2 mentions without citation

Structural evidence for substrate-induced synergism and half-sites reactivity in biotin carboxylase.
Mochalkin et al. (2008)
1 more