› 3a7r

X-ray diffraction
2.05Å resolution

Crystal structure of E. coli lipoate-protein ligase A in complex with lipoyl-AMP.

Released:
DOI: 10.2210/pdb3a7r/pdb
PDB entry 3a7r coloured by chain, front view.
PDB entry 3a7r coloured by chain, side view.
PDB entry 3a7r coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Global conformational change associated with the two-step reaction catalyzed by Escherichia coli lipoate-protein ligase A.
Fujiwara K, Maita N, Hosaka H, Okamura-Ikeda K, Nakagawa A, Taniguchi H
J Biol Chem 285 9971-9980 (2010)
PMID: 20089862

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152202 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lipoate-protein ligase A Chain: A
Molecule details ›
Chain: A
Length: 337 amino acids
Theoretical weight: 37.84 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P32099 (Residues: 2-338; Coverage: 100%)
Gene names: JW4349, b4386, lplA, yjjF
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand LAQ 1 x LAQ
Ligand SO4 4 x SO4
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-17A
Spacegroup: P6122
Unit cell:
a: 102.298Å b: 102.298Å c: 221.252Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.177 0.176 0.204
Expression system: Escherichia coli

Quick links

Citations

7 review citations

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

8 mentions without citation

Computational design of a red fluorophore ligase for site-specific protein labeling in living cells.
Liu et al. (2014)
7 more