Molecular mechanism of SbmA, a promiscuous transporter exploited by antimicrobial peptides
| Autor: | Elizabeth Michalczyk, Konstantinos Beis, Graham C. Walker, Sylvie Rebuffat, Feng Qu, Dmitry Ghilarov, Zuzanna Pakosz, Piotr Stepien, Satoshi Ogasawara, Norimichi Nomura, Jonathan G. Heddle, So Iwata, Satomi Inaba-Inoue |
|---|---|
| Přispěvatelé: | Japan Society for the Promotion of Science, Biotechnology and Biological Sciences Research Council (BBSRC), Uniwersytet Jagielloński w Krakowie = Jagiellonian University (UJ), Imperial College London, Kyoto University [Kyoto], Massachusetts Institute of Technology (MIT), Molécules de Communication et Adaptation des Micro-organismes (MCAM), Muséum national d'Histoire naturelle (MNHN)-Centre National de la Recherche Scientifique (CNRS) |
| Rok vydání: | 2021 |
| Předmět: |
0303 health sciences
Multidisciplinary 030306 microbiology Chemistry medicine.drug_class media_common.quotation_subject [SDV.BA]Life Sciences [q-bio]/Animal biology Antimicrobial peptides Antibiotics Transporter Competition (biology) 3. Good health 03 medical and health sciences Biochemistry medicine Molecular mechanism Bacterial outer membrane 030304 developmental biology media_common |
| Zdroj: | Science Advances Science Advances, American Association for the Advancement of Science (AAAS), 2021, 7 (37), ⟨10.1126/sciadv.abj5363⟩ |
| ISSN: | 2375-2548 |
| DOI: | 10.1126/sciadv.abj5363⟩ |
| Popis: | 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 Å 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. 抗菌ペプチドは細菌の細胞内にどのように取り込まれるのか？ --細菌の膜輸送体SbmAの立体構造の解明--. 京都大学プレスリリース. 2021-09-09. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|