Structural highlights
Function
[R0BTE9_9FIRM] First step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan.[HAMAP-Rule:MF_00038]
Publication Abstract from PubMed
The 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
- ↑ Hakulinen JK, Hering J, Branden G, Chen H, Snijder A, Ek M, Johansson P. MraY-antibiotic complex reveals details of tunicamycin mode of action. Nat Chem Biol. 2017 Jan 9. doi: 10.1038/nchembio.2270. PMID:28068312 doi:http://dx.doi.org/10.1038/nchembio.2270
