› 1x2h

X-ray diffraction
2.91Å resolution

Crystal Structure of Lipate-Protein Ligase A from Escherichia coli complexed with lipoic acid

Released:
DOI: 10.2210/pdb1x2h/pdb
PDB entry 1x2h coloured by chain, front view.
PDB entry 1x2h coloured by chain, side view.
PDB entry 1x2h coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structure of lipoate-protein ligase A from Escherichia coli. Determination of the lipoic acid-binding site.
Fujiwara K, Toma S, Okamura-Ikeda K, Motokawa Y, Nakagawa A, Taniguchi H
J Biol Chem 280 33645-51 (2005)
PMID: 16043486

Function and Biology Details

Reaction catalysed: 
(1a) ATP + (R)-lipoate = lipoyl-AMP + diphosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure 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 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 337 amino acids
Theoretical weight: 38.08 KDa
Source organism: Escherichia coli
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

1 bound ligand:
Ligand LPA 2 x LPA
1 modified residue:
Ligand MSE 15 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: C2221
Unit cell:
a: 83.2Å b: 111.6Å c: 289.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.186 0.271
Expression system: Escherichia coli

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Citations

9 review citations

Glycine cleavage system: reaction mechanism, physiological significance, and hyperglycinemia.
Kikuchi et al. (2008)
8 more

6 mentions without citation

Yeast display evolution of a kinetically efficient 13-amino acid substrate for lipoic acid ligase.
Puthenveetil et al. (2009)
5 more