› 2vpq

X-ray diffraction
2.1Å resolution

Crystal structure of biotin carboxylase from S. aureus complexed with AMPPNP

Released:
DOI: 10.2210/pdb2vpq/pdb
PDB entry 2vpq coloured by chain, front view.
PDB entry 2vpq coloured by chain, side view.
PDB entry 2vpq coloured by chain, top view.
Source organism: Staphylococcus aureus
Primary publication:
Structural evidence for substrate-induced synergism and half-sites reactivity in biotin carboxylase.
Mochalkin I, Miller JR, Evdokimov A, Lightle S, Yan C, Stover CK, Waldrop GL
Protein Sci 17 1706-18 (2008)
PMID: 18725455

Function and Biology Details

Reaction catalysed: 
ATP + [biotin carboxyl-carrier protein]-biotin-N(6)-L-lysine + hydrogencarbonate- = ADP + phosphate + [biotin carboxyl-carrier protein]-carboxybiotin-N(6)-L-lysine
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-101944 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Biotin carboxylase Chains: A, B
Molecule details ›
Chains: A, B
Length: 451 amino acids
Theoretical weight: 50.11 KDa
Source organism: Staphylococcus aureus
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A0H3JRR2 (Residues: 1-451; Coverage: 100%)
Gene names: SAV1526, accC
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand ANP 2 x ANP
Ligand MG 4 x MG
Ligand CL 2 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P21
Unit cell:
a: 78.247Å b: 63.318Å c: 105.142Å
α: 90° β: 103.82° γ: 90°
R-values:
R R work R free
0.219 0.215 0.284
Expression system: Escherichia coli

Quick links

Citations

5 review citations

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

7 mentions without citation

The enzymes of biotin dependent CO₂ metabolism: what structures reveal about their reaction mechanisms.
Waldrop et al. (2012)
6 more