2olu | pdb_00002olu
|
Structural Insight Into the Transglycosylation Step Of Bacterial Cell Wall Biosynthesis : Apoenzyme
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
2OLU is a Single protein structure of sequence from Staphylococcus aureus with EDO 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
Page seeded by OCA on Tue Jan 29 21:13:04 2008
