3S2U

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

Summary for 3S2U

• Entry DOI: 10.2210/pdb3s2u/pdb
• Descriptor: UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase, URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE (3 entities in total)
• Functional Keywords: n-acetylglucosaminyl transferase, transferase
• Biological source: Pseudomonas aeruginosa
• Cellular location: Cell inner membrane; Peripheral membrane protein (By similarity): Q9HW01
• Total number of polymer chains: 1
• Total formula weight: 39526.41

Authors

Brown, K.,Vial, S.C.M.,Dedi, N.,Westcott, J.,Scally, S.,Bugg, T.D.H.,Charlton, P.A.,Cheetham, G.M.T. (deposition date: 2011-05-17, release date: 2012-09-26, Last modification date: 2024-02-28)

Primary citation

Brown, K.,Vial, S.C.,Dedi, N.,Westcott, J.,Scally, S.,Bugg, T.D.,Charlton, P.A.,Cheetham, G.M.
Crystal Structure of the Pseudomonas aeruginosa MurG: UDP-GlcNAc Substrate Complex.
Protein Pept.Lett., 20:1002-1008, 2013

PubMed Abstract: 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.

PubMed: 22973843

Experimental method

X-RAY DIFFRACTION (2.23 Å)