› 1dv1

X-ray diffraction
1.9Å resolution

STRUCTURE OF BIOTIN CARBOXYLASE (APO)

Released:
DOI: 10.2210/pdb1dv1/pdb
PDB entry 1dv1 coloured by chain, front view.
PDB entry 1dv1 coloured by chain, side view.
PDB entry 1dv1 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Movement of the biotin carboxylase B-domain as a result of ATP binding.
Thoden JB, Blanchard CZ, Holden HM, Waldrop GL
J Biol Chem 275 16183-90 (2000)
PMID: 10821865

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:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150166 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Biotin carboxylase Chains: A, B
Molecule details ›
Chains: A, B
Length: 449 amino acids
Theoretical weight: 49.39 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P24182 (Residues: 1-449; Coverage: 100%)
Gene names: JW3224, accC, b3256, fabG
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand PO4 2 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 61.7Å b: 95.8Å c: 180.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.18 0.238
Expression system: Escherichia coli

Quick links

Citations

15 review citations

Multi-subunit acetyl-CoA carboxylases.
Cronan et al. (2002)
14 more

9 mentions without citation

Divergence and convergence in enzyme evolution.
Galperin et al. (2012)
8 more