› 2d5d

X-ray diffraction
1.55Å resolution

Structure of Biotin Carboxyl Carrier Protein (74Val start) from Pyrococcus horikoshi OT3 Ligand Free Form II

Released:
DOI: 10.2210/pdb2d5d/pdb
PDB entry 2d5d coloured by chain, front view.
PDB entry 2d5d coloured by chain, side view.
PDB entry 2d5d coloured by chain, top view.
Source organism: Pyrococcus horikoshii OT3
Primary publication:
Protein biotinylation visualized by a complex structure of biotin protein ligase with a substrate.
Bagautdinov B, Matsuura Y, Bagautdinova S, Kunishima N
J Biol Chem 283 14739-50 (2008)
PMID: 18372281

Function and Biology Details

Reaction catalysed: 
(S)-methylmalonyl-CoA + pyruvate = propanoyl-CoA + oxaloacetate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129796 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lipoyl-binding domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 74 amino acids
Theoretical weight: 7.99 KDa
Source organism: Pyrococcus horikoshii OT3
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O59021 (Residues: 77-149; Coverage: 49%)
Gene name: PH1284
Sequence domains: Biotin-requiring enzyme
Structure domains: OB fold (Dihydrolipoamide Acetyltransferase, E2P)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B1
Spacegroup: P212121
Unit cell:
a: 39.689Å b: 39.765Å c: 88.418Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.254 0.254 0.264
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

Modulation of epigenetic targets for anticancer therapy: clinicopathological relevance, structural data and drug discovery perspectives.
Andreoli et al. (2013)
5 more

2 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)
1 more