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1: Science. 2007 Mar 9;315(5817):1402-5.Click here to read Links
Comment in:
Science. 2007 Mar 9;315(5817):1373-4.

Structural insight into the transglycosylation step of bacterial cell-wall biosynthesis.

Lovering AL, de Castro LH, Lim D, Strynadka NC.

Department of Biochemistry and Molecular Biology, and Center for Blood Research, University of British Columbia, 2350 Health Sciences Mall, Vancouver, Canada.

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.

PMID: 17347437 [PubMed - indexed for MEDLINE]

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