› 2art

X-ray diffraction
2.4Å resolution

Crystal structure of lipoate-protein ligase A bound with lipoyl-AMP

Released:
DOI: 10.2210/pdb2art/pdb
PDB entry 2art coloured by chain, front view.
PDB entry 2art coloured by chain, side view.
PDB entry 2art coloured by chain, top view.
Source organism: Thermoplasma acidophilum
Primary publication:
Crystal structure of lipoate-protein ligase A bound with the activated intermediate: insights into interaction with lipoyl domains.
Kim DJ, Kim KH, Lee HH, Lee SJ, Ha JY, Yoon HJ, Suh SW
J Biol Chem 280 38081-9 (2005)
PMID: 16141198

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 Chain: A
Molecule details ›
Chain: A
Length: 262 amino acids
Theoretical weight: 29.92 KDa
Source organism: Thermoplasma acidophilum
Expression system: Escherichia coli
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

3 bound ligands:
Ligand MG 1 x MG
Ligand LPA 1 x LPA
Ligand AMP 1 x AMP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: C2
Unit cell:
a: 108.459Å b: 62.715Å c: 46.408Å
α: 90° β: 111.1° γ: 90°
R-values:
R R work R free
0.197 0.197 0.253
Expression system: Escherichia coli

Quick links

Citations

3 review citations

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

5 mentions without citation

Advances in synthesis of biotin and assembly of lipoic acid.
Cronan JE. (2018)
4 more