2c6w
From Proteopedia
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[[Category: peptidoglycan synthesis]] | [[Category: peptidoglycan synthesis]] | ||
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Revision as of 14:55, 30 October 2007
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PENICILLIN-BINDING PROTEIN 1A (PBP-1A) FROM STREPTOCOCCUS PNEUMONIAE
Overview
Streptococcus pneumoniae is a major human pathogen whose infections have, been treated with beta-lactam antibiotics for over 60 years, but the, proliferation of strains that are highly resistant to such drugs is a, problem of worldwide concern. Beta-lactams target penicillin-binding, proteins (PBPs), membrane-associated enzymes that play essential roles in, the peptidoglycan biosynthetic process. Bifunctional PBPs catalyze both, the polymerization of glycan chains (glycosyltransfer) and the, cross-linking of adjacent pentapeptides (transpeptidation), while, monofunctional enzymes catalyze only the latter reaction. Although S., pneumoniae has six PBPs, only three (PBP1a, PBP2x, PBP2b) are major, resistance determinants, with PBP1a being the only bifunctional enzyme., PBP1a plays a key role ... [(full description)]
About this Structure
2C6W is a [Protein complex] structure of sequences from [Streptococcus pneumoniae] with ZN and CL as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Crystal structure of penicillin-binding protein 1a (PBP1a) reveals a mutational hotspot implicated in beta-lactam resistance in Streptococcus pneumoniae., Contreras-Martel C, Job V, Di Guilmi AM, Vernet T, Dideberg O, Dessen A, J Mol Biol. 2006 Jan 27;355(4):684-96. Epub 2005 Nov 9. PMID:16316661
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