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TitleStructural and functional insights into the delivery of a bacterial Rhs pore-forming toxin to the membrane.
Journal, issue, pagesNat Commun, Vol. 14, Issue 1, Page 7808, Year 2023
Publish dateNov 28, 2023
AuthorsAmaia 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 AbstractBacterial 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.
External linksNat Commun / PubMed:38016939 / PubMed Central
MethodsEM (single particle)
Resolution2.45 Å
Structure data

16778

8cp6

EMDB-16778, PDB-8cp6:
Type six secretion system exported effector 5 (Tse5)
Method: EM (single particle) / Resolution: 2.45 Å

Source
  • Pseudomonas (RNA similarity group I)
  • pseudomonas aeruginosa (bacteria)
KeywordsTOXIN / Pore-forming protein / P.aeruginosa / effector / Bacterial Rearrangement hot spot protein / ion channel / type VI secretion system

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