Structural studies of the novel antibacterial target MraY and its interaction with the natural inhibitor compound tunicamycin

2^nd International Conference on PHARMACEUTICAL CHEMISTRY

October 02-04, 2017 Barcelona, Spain

Gisela Branden

University of Gothenburg, Sweden

Scientific Tracks Abstracts: Med Chem (Los Angeles)

Abstract :

The rapid increase of antibiotic resistance has created an urgent need to develop novel antibacterial drugs. I will describe the crystal structure of the promising bacterial target phospho-N-acetylmuramoyl�pentapeptide translocase (MraY) in complex with the nucleoside antibiotic tunicamycin. The structure reveals the mode of action of several related natural-product antibiotics and also gives an indication on the binding mode of the MraY UDP�MurNAc�pentapeptide and undecaprenyl-phosphate substrates. (Hakulinen et al. Nature Chemical Biology, 13:265-267, 2017)