› 2vqd

X-ray diffraction
2.41Å resolution

Crystal Structure of Biotin Carboxylase from Pseudomonas aeruginosa complexed with AMPCP

Released:
DOI: 10.2210/pdb2vqd/pdb
PDB entry 2vqd coloured by chain, front view.
PDB entry 2vqd coloured by chain, side view.
PDB entry 2vqd coloured by chain, top view.
Source organism: Pseudomonas aeruginosa
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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153487 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Biotin carboxylase Chain: A
Molecule details ›
Chain: A
Length: 464 amino acids
Theoretical weight: 50.78 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli
UniProt:
  • Canonical: P37798 (Residues: 1-449; Coverage: 100%)
Gene names: PA4848, accC, fabG
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand AP2 1 x AP2
Ligand MG 1 x MG
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P21212
Unit cell:
a: 64.227Å b: 126.786Å c: 49.878Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.178 0.252
Expression system: Escherichia coli

Quick links

Citations

6 review citations

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

3 mentions without citation

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