› 2vr1

X-ray diffraction
2.6Å resolution

Crystal structure of Biotin carboxylase from E. coli in complex with ATP analog, ADPCF2P.

Released:
DOI: 10.2210/pdb2vr1/pdb
PDB entry 2vr1 coloured by chain, front view.
PDB entry 2vr1 coloured by chain, side view.
PDB entry 2vr1 coloured by chain, top view.
Source organism: Escherichia coli
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:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150165 (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

2 bound ligands:
Ligand CL 2 x CL
Ligand ATF 1 x ATF
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P212121
Unit cell:
a: 84.129Å b: 106.784Å c: 121.91Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.189 0.247
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

1 mention without citation

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