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TitleThe Structure of Enterococcus Faecium L,D---Transpeptidase Acylated by Ertapenem Provides Insight Into the Inactivation Mechanism.
Journal, issue, pagesAcs Chem. Biol., Vol. 8, Page 1140-, Year 2013
Publish dateDec 14, 2012 (structure data deposition date)
AuthorsLecoq, L. / Dubee, V. / Triboulet, S. / Bougault, C. / Hugonnet, J.E. / Arthur, M. / Simorre, J.P.
External linksAcs Chem. Biol. / PubMed:23574509
MethodsNMR (solution)
Structure data

PDB-3zg4:
NMR structure of the catalytic domain from E. faecium L,D- transpeptidase
Method: SOLUTION NMR

PDB-3zgp:
NMR structure of the catalytic domain from E. faecium L,D- transpeptidase acylated by ertapenem
Method: SOLUTION NMR

Chemicals

ChemComp-1RG:
(4R,5S)-3-({(3S,5S)-5-[(3-carboxyphenyl)carbamoyl]pyrrolidin-3-yl}sulfanyl)-5-[(1S,2R)-1-formyl-2-hydroxypropyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid / medication, antibiotic*YM

Source
  • enterococcus faecium (bacteria)
KeywordsTRANSFERASE / TRANSPEPTIDATION / PEPTIDOGLYCAN BIOSYNTHESIS / ANTIBIOTIC RESISTANCE

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