3S2U

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

3S2U の概要

• エントリーDOI: 10.2210/pdb3s2u/pdb
• 分子名称: UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase, URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE (3 entities in total)
• 機能のキーワード: n-acetylglucosaminyl transferase, transferase
• 由来する生物種: Pseudomonas aeruginosa
• 細胞内の位置: Cell inner membrane; Peripheral membrane protein (By similarity): Q9HW01
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 39526.41

構造登録者

Brown, K.,Vial, S.C.M.,Dedi, N.,Westcott, J.,Scally, S.,Bugg, T.D.H.,Charlton, P.A.,Cheetham, G.M.T. (登録日: 2011-05-17, 公開日: 2012-09-26, 最終更新日: 2024-02-28)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.23 Å)