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X-ray diffraction
2.3Å resolution

Biotin protein ligase from Aquifex aeolicus in complex with biotin and ATP

Released:
DOI: 10.2210/pdb3efs/pdb
PDB entry 3efs coloured by chain, front view.
PDB entry 3efs coloured by chain, side view.
PDB entry 3efs coloured by chain, top view.
Source organism: Aquifex aeolicus
Primary publication:
Structural and functional studies of the biotin protein ligase from Aquifex aeolicus reveal a critical role for a conserved residue in target specificity.
Tron CM, McNae IW, Nutley M, Clarke DJ, Cooper A, Walkinshaw MD, Baxter RL, Campopiano DJ
J Mol Biol 387 129-46 (2009)
PMID: 19385043

Function and Biology Details

Reaction catalysed: 
ATP + biotin + [biotin carboxyl-carrier protein]-L-lysine = AMP + diphosphate + [biotin carboxyl-carrier protein]-N(6)-biotinyl-L-lysine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130387 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
biotin--[biotin carboxyl-carrier protein] ligase Chains: A, B
Molecule details ›
Chains: A, B
Length: 233 amino acids
Theoretical weight: 26.75 KDa
Source organism: Aquifex aeolicus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O66837 (Residues: 1-233; Coverage: 100%)
Gene names: aq_566, birA
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand BTN 2 x BTN
2 bound ligands:
Ligand ATP 2 x ATP
Ligand SO4 3 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P212121
Unit cell:
a: 41.225Å b: 81.695Å c: 143.278Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.232 0.23 0.264
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

Survey of the year 2009: applications of isothermal titration calorimetry.
Falconer et al. (2011)
3 more

5 mentions without citation

Proximity Dependent Biotinylation: Key Enzymes and Adaptation to Proteomics Approaches.
Samavarchi-Tehrani et al. (2020)
4 more