| Literature DB >> 28068312 |
Jonna K Hakulinen1, Jenny Hering1,2, Gisela Brändén2, Hongming Chen1, Arjan Snijder1, Margareta Ek1, Patrik Johansson1.
Abstract
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.Entities:
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Year: 2017 PMID: 28068312 DOI: 10.1038/nchembio.2270
Source DB: PubMed Journal: Nat Chem Biol ISSN: 1552-4450 Impact factor: 15.040