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Title: Molecular mechanism of SbmA, a promiscuous transporter exploited by antimicrobial peptides
Authors: Ghilarov, Dmitry
Inaba-Inoue, Satomi
Stepien, Piotr
Qu, Feng
Michalczyk, Elizabeth
Pakosz, Zuzanna
Nomura, Norimichi  kyouindb  KAKEN_id
Ogasawara, Satoshi
Walker, Graham Charles
Rebuffat, Sylvie
Iwata, So
Heddle, Jonathan Gardiner
Beis, Konstantinos
Author's alias: 稲葉, 理美
野村, 紀通
小笠原, 諭
岩田, 想
Issue Date: Sep-2021
Publisher: American Association for the Advancement of Science (AAAS)
Journal title: Science Advances
Volume: 7
Issue: 37
Thesis number: eabj5363
Abstract: 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.
Description: 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.
Rights: Copyright © 2021 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution NonCommercial License 4.0 (CC BY-NC).
This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial license, which permits use, distribution, and reproduction in any medium, so long as the resultant use is not for commercial advantage and provided the original work is properly cited.
URI: http://hdl.handle.net/2433/265258
DOI(Published Version): 10.1126/sciadv.abj5363
PubMed ID: 34516884
Related Link: https://www.kyoto-u.ac.jp/ja/research-news/2021-09-09-0
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