Structural highlights
Evolutionary Conservation
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Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lovering AL, de Castro LH, Lim D, Strynadka NC. Structural insight into the transglycosylation step of bacterial cell-wall biosynthesis. Science. 2007 Mar 9;315(5817):1402-5. PMID:17347437 doi:315/5817/1402
