2c8m

X-ray diffraction
1.89Å resolution

Structure of protein Ta0514, putative lipoate protein ligase from T. acidophilum with bound lipoic acid

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
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: Lipoyl protein ligase A/B catalytic domain
Structure domains: Bira Bifunctional Protein; Domain 2

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P21
Unit cell:
a: 53.377Å b: 117.882Å c: 105.663Å
α: 90° β: 93.51° γ: 90°
R-values:
R R work R free
0.208 0.207 0.239
Expression system: Escherichia coli BL21(DE3)