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Structure paper

TitleGlobal conformational change associated with the two-step reaction catalyzed by Escherichia coli lipoate-protein ligase A.
Journal, issue, pagesJ. Biol. Chem., Vol. 285, Page 9971-9980, Year 2010
Publish dateSep 20, 2009 (structure data deposition date)
AuthorsFujiwara, K. / Maita, N. / Hosaka, H. / Okamura-Ikeda, K. / Nakagawa, A. / Taniguchi, H.
External linksJ. Biol. Chem. / PubMed:20089862
MethodsX-ray diffraction
Resolution1.3 - 3.44 Å
Structure data

PDB-3a7a:
Crystal structure of E. coli lipoate-protein ligase A in complex with octyl-amp and apoH-protein
Method: X-RAY DIFFRACTION / Resolution: 3.1 Å

PDB-3a7l:
Crystal structure of E. coli apoH-protein
Method: X-RAY DIFFRACTION / Resolution: 1.3 Å

PDB-3a7r:
Crystal structure of E. coli lipoate-protein ligase A in complex with lipoyl-AMP.
Method: X-RAY DIFFRACTION / Resolution: 2.05 Å

PDB-3a7u:
Crystal structure of the bovine lipoyltransferase in its unliganded form
Method: X-RAY DIFFRACTION / Resolution: 3.44 Å

Chemicals

ChemComp-OCT:
N-OCTANE

ChemComp-AMP:
ADENOSINE MONOPHOSPHATE / AMP*YM

ChemComp-HOH:
WATER

ChemComp-LAQ:
5'-O-[(R)-({5-[(3R)-1,2-DITHIOLAN-3-YL]PENTANOYL}OXY)(HYDROXY)PHOSPHORYL]ADENOSINE

ChemComp-SO4:
SULFATE ION

ChemComp-MG:
Unknown entry

Source
  • escherichia coli (E. coli)
  • bos taurus (cattle)
KeywordsLIGASE / ADENIYLATE-FORMING ENZYME / ATP-binding / Nucleotide-binding / Transferase / Lipoyl / TRANSPORT PROTEIN / glycine cleavage system / lipoic acid / ADENYLATE-FORMING ENZYME / Cytoplasm / Acyltransferase / Mitochondrion / Transit peptide

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