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Structural basis for selective inhibition of antibacterial target MraY, a membrane-bound enzyme involved in peptidoglycan synthesis

Review article
Authors Jenny Hering
Elin Dunevall
Margareta Ek
Gisela Brändén
Published in Drug Discovery Today
Volume 23
Issue 7
Pages 1426-1435
ISSN 13596446
Publication year 2018
Published at Department of Chemistry and Molecular Biology
Pages 1426-1435
Language en
Links https://doi.org/10.1016/j.drudis.20...
Keywords structure-based drug design, membrane protein, antibiotic resistance
Subject categories Biochemistry, Structural Biology

Abstract

The rapid growth of antibiotic-resistant bacterial infections is of major concern for human health. Therefore, it is of great importance to characterize novel targets for the development of antibacterial drugs. One promising protein target is MraY (UDP-N-acetylmuramyl-pentapeptide: undecaprenyl phosphate N-acetylmuramyl-pentapeptide-1-phosphate transferase or MurNAc-1-P-transferase), which is essential for bacterial cell wall synthesis. Here, we summarize recent breakthroughs in structural studies of bacterial MraYs and the closely related human GPT (UDP-N-acetylglucosamine: dolichyl phosphate N-acetylglucosamine-1-phosphate transferase or GlcNAc-1-P-transferase). We present a detailed comparison of interaction modes with the natural product inhibitors tunicamycin and muraymycin D2. Finally, we speculate on possible routes to design an antibacterial agent in the form of a potent and selective inhibitor against MraY.

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