› 4op0

X-ray diffraction
1.7Å resolution

Crystal structure of biotin protein ligase (RV3279C) of Mycobacterium tuberculosis, complexed with biotinyl-5'-AMP

Released:
DOI: 10.2210/pdb4op0/pdb
PDB entry 4op0 coloured by chain, front view.
PDB entry 4op0 coloured by chain, side view.
PDB entry 4op0 coloured by chain, top view.
Source organism: Mycobacterium tuberculosis H37Rv
Primary publication:
Active site conformational changes upon reaction intermediate biotinyl-5'-AMP binding in biotin protein ligase from Mycobacterium tuberculosis.
Ma Q, Akhter Y, Wilmanns M, Ehebauer MT
Protein Sci 23 932-9 (2014)
PMID: 24723382

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-125216 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Biotin--[acetyl-CoA-carboxylase] ligase Chains: A, B
Molecule details ›
Chains: A, B
Length: 268 amino acids
Theoretical weight: 28.25 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: I6YFP0 (Residues: 3-266; Coverage: 99%)
Gene names: Rv3279c, birA
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand BT5 2 x BT5
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7A
Spacegroup: P21
Unit cell:
a: 41.737Å b: 75.406Å c: 77.599Å
α: 90° β: 97.92° γ: 90°
R-values:
R R work R free
0.194 0.192 0.242
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Mechanisms Governing Precise Protein Biotinylation.
Sternicki et al. (2017)
4 other articles

3 mentions without citation

Active site conformational changes upon reaction intermediate biotinyl-5'-AMP binding in biotin protein ligase from Mycobacterium tuberculosis.
Ma et al. (2014)
2 more