2jch: Difference between revisions
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[[Category: peptidoglycan synthesis multifunctional enzyme]] | [[Category: peptidoglycan synthesis multifunctional enzyme]] | ||
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Revision as of 18:25, 30 October 2007
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STRUCTURAL AND MECHANISTIC BASIS OF PENICILLIN BINDING PROTEIN INHIBITION BY LACTIVICINS
OverviewOverview
beta-lactam antibiotics, including penicillins and cephalosporins, inhibit, penicillin-binding proteins (PBPs), which are essential for bacterial cell, wall biogenesis. Pathogenic bacteria have evolved efficient antibiotic, resistance mechanisms that, in Gram-positive bacteria, include mutations, to PBPs that enable them to avoid beta-lactam inhibition. Lactivicin (LTV;, 1) contains separate cycloserine and gamma-lactone rings and is the only, known natural PBP inhibitor that does not contain a beta-lactam. Here we, show that LTV and a more potent analog, phenoxyacetyl-LTV (PLTV; 2), are, active against clinically isolated, penicillin-resistant Streptococcus, pneumoniae strains. Crystallographic analyses of S. pneumoniae PBP1b, reveal that LTV and PLTV inhibition involves opening of both ... [(full description)]
About this StructureAbout this Structure
2JCH is a [Single protein] structure of sequence from [Streptococcus pneumoniae r6] with SO4, CL, EDO and PL7 as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Structural and mechanistic basis of penicillin-binding protein inhibition by lactivicins., Macheboeuf P, Fischer DS, Brown T Jr, Zervosen A, Luxen A, Joris B, Dessen A, Schofield CJ, Nat Chem Biol. 2007 Aug 5;. PMID:17676039
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