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-Structure paper
タイトル | Structural and functional insights into the delivery of a bacterial Rhs pore-forming toxin to the membrane. |
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ジャーナル・号・ページ | Nat Commun, Vol. 14, Issue 1, Page 7808, Year 2023 |
掲載日 | 2023年11月28日 |
著者 | Amaia González-Magaña / Igor Tascón / Jon Altuna-Alvarez / María Queralt-Martín / Jake Colautti / Carmen Velázquez / Maialen Zabala / Jessica Rojas-Palomino / Marité Cárdenas / Antonio Alcaraz / John C Whitney / Iban Ubarretxena-Belandia / David Albesa-Jové / |
PubMed 要旨 | Bacterial competition is a significant driver of toxin polymorphism, which allows continual compensatory evolution between toxins and the resistance developed to overcome their activity. Bacterial ...Bacterial competition is a significant driver of toxin polymorphism, which allows continual compensatory evolution between toxins and the resistance developed to overcome their activity. Bacterial Rearrangement hot spot (Rhs) proteins represent a widespread example of toxin polymorphism. Here, we present the 2.45 Å cryo-electron microscopy structure of Tse5, an Rhs protein central to Pseudomonas aeruginosa type VI secretion system-mediated bacterial competition. This structural insight, coupled with an extensive array of biophysical and genetic investigations, unravels the multifaceted functional mechanisms of Tse5. The data suggest that interfacial Tse5-membrane binding delivers its encapsulated pore-forming toxin fragment to the target bacterial membrane, where it assembles pores that cause cell depolarisation and, ultimately, bacterial death. |
リンク | Nat Commun / PubMed:38016939 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 2.45 Å |
構造データ | EMDB-16778, PDB-8cp6: |
由来 |
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キーワード | TOXIN / Pore-forming protein / P.aeruginosa / effector / Bacterial Rearrangement hot spot protein / ion channel / type VI secretion system |