› 2c7i

X-ray diffraction
2.1Å resolution

Structure of protein Ta0514, putative lipoate protein ligase from T. acidophilum.

Released:
DOI: 10.2210/pdb2c7i/pdb
PDB entry 2c7i coloured by chain, front view.
PDB entry 2c7i coloured by chain, side view.
PDB entry 2c7i coloured by chain, top view.
Source organism: Thermoplasma acidophilum DSM 1728
Primary publication:
Structure of a putative lipoate protein ligase from Thermoplasma acidophilum and the mechanism of target selection for post-translational modification.
McManus E, Luisi BF, Perham RN
J Mol Biol 356 625-37 (2006)
PMID: 16384580

Function and Biology Details

Reaction catalysed: 
(1a) ATP + (R)-lipoate = lipoyl-AMP + diphosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190879 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lipoate-protein ligase A subunit 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 262 amino acids
Theoretical weight: 29.92 KDa
Source organism: Thermoplasma acidophilum DSM 1728
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9HKT1 (Residues: 1-262; Coverage: 100%)
Gene names: Ta0514, lplA
Sequence domains: Biotin/lipoate A/B protein ligase family
Structure domains: Bira Bifunctional Protein; Domain 2

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P21
Unit cell:
a: 53.23Å b: 118.356Å c: 105.592Å
α: 90° β: 93.75° γ: 90°
R-values:
R R work R free
0.21 0.208 0.252
Expression system: Escherichia coli BL21(DE3)

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Citations

4 review citations

Lipoic acid metabolism in microbial pathogens.
Spalding et al. (2010)
3 more