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X-ray diffraction
1.6Å resolution

Crystal Structure Of Biotin-(Acetyl-CoA-Carboxylase) ligase From Pyrococcus Horikoshii Ot3 in complex with biotin

Released:
DOI: 10.2210/pdb1wpy/pdb
PDB entry 1wpy coloured by chain, front view.
PDB entry 1wpy coloured by chain, side view.
PDB entry 1wpy coloured by chain, top view.
Source organism: Pyrococcus horikoshii OT3
Primary publication:
Crystal structures of biotin protein ligase from Pyrococcus horikoshii OT3 and its complexes: structural basis of biotin activation.
Bagautdinov B, Kuroishi C, Sugahara M, Kunishima N
J Mol Biol 353 322-33 (2005)
PMID: 16169557

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 domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129627 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
BPL/LPL catalytic domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 235 amino acids
Theoretical weight: 26.34 KDa
Source organism: Pyrococcus horikoshii OT3
Expression system: Escherichia coli
UniProt:
  • Canonical: O57883 (Residues: 1-235; Coverage: 100%)
Gene name: PH0147
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand BTN 2 x BTN
No bound ligands
1 modified residue:
Ligand MSE 10 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B1
Spacegroup: P21
Unit cell:
a: 38.42Å b: 82.737Å c: 72.711Å
α: 90° β: 103.17° γ: 90°
R-values:
R R work R free
0.194 0.194 0.213
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Vitamin and cofactor biosynthesis pathways in Plasmodium and other apicomplexan parasites.
Müller et al. (2007)
3 more

4 mentions without citation

Structural ordering of disordered ligand-binding loops of biotin protein ligase into active conformations as a consequence of dehydration.
Gupta et al. (2010)
3 more