AI Article Synopsis
- The rise of antibiotic-resistant bacterial infections is a serious public health issue, highlighting the need for new antibacterial drug targets.
- MraY, a crucial protein for bacterial cell wall synthesis, has emerged as a promising target for drug development.
- Recent research on MraY and its related human protein, GPT, has revealed how they interact with natural inhibitors, which could inform the design of effective new antibacterial agents.
Article 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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| http://dx.doi.org/10.1016/j.drudis.2018.05.020 | DOI Listing |
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