4.8 Article

Molecular mechanism of SbmA, a promiscuous transporter exploited by antimicrobial peptides

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SCIENCE ADVANCES
卷 7, 期 37, 页码 -

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AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/sciadv.abj5363

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资金

  1. Biotechnology and Biological Sciences Research Council [BB/H01778X/1]
  2. Team program of the Foundation for Polish Science
  3. European Union under the European Regional Development Fund [TEAM/2016-3/23]
  4. National Science Centre (NCN, Poland) [2016/21/B/CC1/00274, 2019/35/D/NZ1/01770]
  5. Chinese Scholarship Council Scheme
  6. Japan Society for the Promotion of Science Overseas Fellowship
  7. Basis for Supporting Innovative Drug Discovery and Life Science Research (BINDS) from the Japan Agency of Medical Research and Development (AMED) [20am0101079]
  8. Research on Development of New Drugs from the AMED
  9. National Institutes of Health (NIH) [GM31030]
  10. BioS Priority Research Area under the program Excellence Initiative Research University at the Jagiellonian University in Krakow

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Antibiotic metabolites and antimicrobial peptides play a key role in bacterial competition by entering cells through hijacking membrane proteins. The newly discovered SbmA-like peptide transporters provide insight into the molecular mechanism of peptide uptake, potentially leading to the development of targeted therapeutics.
Antibiotic metabolites and antimicrobial peptides mediate competition between bacterial species. Many of them hijack inner and outer membrane proteins to enter cells. Sensitivity of enteric bacteria to multiple peptide antibiotics is controlled by the single inner membrane protein SbmA. To establish the molecular mechanism of peptide transport by SbmA and related BacA, we determined their cryo-electron microscopy structures at 3.2 and 6 A local resolution, respectively. The structures show a previously unknown fold, defining a new class of secondary transporters named SbmA-like peptide transporters. The core domain includes conserved glutamates, which provide a pathway for proton translocation, powering transport. The structures show an outward-open conformation with a large cavity that can accommodate diverse substrates. We propose a molecular mechanism for antibacterial peptide uptake paving the way for creation of narrow-targeted therapeutics.

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