5jnq
From Proteopedia
MraY tunicamycin complex
Structural highlights
FunctionR0BTE9_9FIRM First step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan.[HAMAP-Rule:MF_00038] Publication Abstract from PubMedThe rapid increase of antibiotic resistance has created an urgent need to develop novel antimicrobial agents. Here we describe the crystal structure of the promising bacterial target phospho-N-acetylmuramoyl-pentapeptide translocase (MraY) in complex with the nucleoside antibiotic tunicamycin. The structure not only reveals the mode of action of several related natural-product antibiotics but also gives an indication on the binding mode of the MraY UDP-MurNAc-pentapeptide and undecaprenyl-phosphate substrates. MraY-antibiotic complex reveals details of tunicamycin mode of action.,Hakulinen JK, Hering J, Branden G, Chen H, Snijder A, Ek M, Johansson P Nat Chem Biol. 2017 Jan 9. doi: 10.1038/nchembio.2270. PMID:28068312[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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