7P34

Cryo-EM structure of the proton-dependent antibacterial peptide transporter SbmA-FabS11-1 in nanodiscs

7P34 の概要

• エントリーDOI: 10.2210/pdb7p34/pdb
• EMDBエントリー: 13168
• 分子名称: Peptide antibiotic transporter SbmA, (1R)-2-{[(S)-{[(2S)-2,3-dihydroxypropyl]oxy}(hydroxy)phosphoryl]oxy}-1-[(hexadecanoyloxy)methyl]ethyl (9Z)-octadec-9-enoate (2 entities in total)
• 機能のキーワード: slipt, proton transport, peptide transport, antibiotics, transport protein
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 94490.09

構造登録者

Ghilarov, D.,Beis, K. (登録日: 2021-07-07, 公開日: 2021-09-15, 最終更新日: 2024-07-17)

主引用文献

Ghilarov, D.,Inaba-Inoue, S.,Stepien, P.,Qu, F.,Michalczyk, E.,Pakosz, Z.,Nomura, N.,Ogasawara, S.,Walker, G.C.,Rebuffat, S.,Iwata, S.,Heddle, J.G.,Beis, K.
Molecular mechanism of SbmA, a promiscuous transporter exploited by antimicrobial peptides.
Sci Adv, 7:eabj5363-eabj5363, 2021

PubMed 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.

PubMed: 34516884
DOI: 10.1126/sciadv.abj5363

実験手法

ELECTRON MICROSCOPY (3.59 Å)