› 3efr

X-ray diffraction
2.55Å resolution

Biotin protein ligase R40G mutant from Aquifex aeolicus in complex with biotin

Released:
DOI: 10.2210/pdb3efr/pdb
PDB entry 3efr coloured by chain, front view.
PDB entry 3efr coloured by chain, side view.
PDB entry 3efr 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: 26.65 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
1 bound ligand:
Ligand SO4 4 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX10.1
Spacegroup: P212121
Unit cell:
a: 41.251Å b: 79.928Å c: 140.173Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.237 0.235 0.289
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

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

3 mentions without citation

Biotin proximity tagging favours unfolded proteins and enables the study of intrinsically disordered regions.
Minde et al. (2020)
2 more