2X71

Structural basis for the interaction of lactivicins with serine beta- lactamases

Summary for 2X71

Entry DOI	10.2210/pdb2x71/pdb
Descriptor	BETA-LACTAMASE, (2E)-2-{[(2S)-2-(ACETYLAMINO)-2-CARBOXYETHOXY]IMINO}PENTANEDIOIC ACID, ETHANOL, ... (5 entities in total)
Functional Keywords	hydrolase-antibiotic complex, antibiotic, hydrolase/antibiotic
Biological source	BACILLUS LICHENIFORMIS
Total number of polymer chains	2
Total formula weight	59597.17
Authors	Sauvage, E.,Herman, R.,Kerff, F.,Rocaboy, M.,Charlier, P. (deposition date: 2010-02-22, release date: 2010-07-14, Last modification date: 2023-12-20)
Primary citation	Brown, T.,Charlier, P.,Herman, R.,Schofield, C.J.,Sauvage, E. Structural Basis for the Interaction of Lactivicins with Serine Beta-Lactamases. J.Med.Chem., 53:5890-, 2010 Cited by PubMed Abstract: Lactivicin (LTV) is a natural non-beta-lactam antibiotic that inhibits penicillin-binding proteins and serine beta-lactamases. A crystal structure of a BS3-LTV complex reveals that, as for its reaction with PBPs, LTV reacts with the nucleophilic serine and that cycloserine and lactone rings of LTV are opened. This structure, together with reported structures of PBP1b with lactivicins, provides a basis for developing improved lactivicin-based gamma-lactam antibiotics. PubMed: 20593835 DOI: 10.1021/JM100437U PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.1 Å)

Structure validation