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Crystal structure of the Pseudomonas aeruginosa MurG:UDP-GlcNAc substrate complexCrystal structure of the Pseudomonas aeruginosa MurG:UDP-GlcNAc substrate complex
Structural highlights
Function[MURG_PSEAE] Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II) (By similarity). Publication Abstract from PubMedMurG 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. Crystal structure of the Pseudomonas aeruginosa MurG:UDP-GlcNAc substrate complex.,Brown K, Vial SC, Dedi N, Westcott J, Scally S, Bugg TD, Charlton PA, Cheetham GM Protein Pept Lett. 2012 Sep 4. PMID:22973843[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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