2olv
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(New page: 200px<br /><applet load="2olv" size="350" color="white" frame="true" align="right" spinBox="true" caption="2olv, resolution 2.800Å" /> '''Structural Insight ...)
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Revision as of 19:13, 29 January 2008
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Structural Insight Into the Transglycosylation Step Of Bacterial Cell Wall Biosynthesis : Donor Ligand Complex
Overview
Peptidoglycan glycosyltransferases (GTs) catalyze the polymerization step, of cell-wall biosynthesis, are membrane-bound, and are highly conserved, across all bacteria. Long considered the "holy grail" of antibiotic, research, they represent an essential and easily accessible drug target, for antibiotic-resistant bacteria, including methicillin-resistant, Staphylococcus aureus. We have determined the 2.8 angstrom structure of a, bifunctional cell-wall cross-linking enzyme, including its transpeptidase, and GT domains, both unliganded and complexed with the substrate analog, moenomycin. The peptidoglycan GTs adopt a fold distinct from those of, other GT classes. The structures give insight into critical features of, the catalytic mechanism and key interactions required for enzyme, inhibition.
About this Structure
2OLV is a Single protein structure of sequence from Staphylococcus aureus with as ligand. Full crystallographic information is available from OCA.
Reference
Structural insight into the transglycosylation step of bacterial cell-wall biosynthesis., Lovering AL, de Castro LH, Lim D, Strynadka NC, Science. 2007 Mar 9;315(5817):1402-5. PMID:17347437
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