Crystal structure of the Pseudomonas aeruginosa MurG: UDP-GlcNAc substrate complex

Murg is an essential bacterial glycosyltransferase enzyme in pseudomonas aeruginosa performing one of the key membrane steps of peptidoglycan synthesis catalyzing the transfer of n-acetyl glucosamine (glcnac) from its donor substrate,udp-glcnac,to the acceptor substrate lipid i. we have solved the crystal structure of the complex between pseudomonas aeruginosa murg and udp-glcnac and compared it with the previously solved complex from e. coli. the structure reveals a large-scale conformational change in the relative orientations of the n-and c-terminal domains,which has the effect of widening the cofactor binding site and displacing the udp-glcnac donor. these results suggest new opportunities to design potent inhibitors of peptidoglycan biosynthesis. © 2013 bentham science publishers.