Published January 17, 2017 | Version v1
Journal article Open

MraY-antibiotic complex reveals details of tunicamycin mode of action

Description

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.

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Funding

European Commission
NANOMEM - Membrane Protein Nanocrystallography 317079
European Commission
X-probe - Advanced XFEL and Synchrotron based Probes of Protein Structure and Dynamics 637295