3s2u | pdb_00003s2u

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

spinqualitylabelsall models 3s2u, resolution 2.23Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3s2u is a 1 chain structure with sequence from Pseudomonas aeruginosa pao1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: UD1 Gene: murG, PA4412 (Pseudomonas aeruginosa PAO1) Activity: Undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase, with EC number 2.4.1.227 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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