8cp6
Type six secretion system exported effector 5 (Tse5)
Structural highlights
FunctionTSE5_PSEAE Toxin secreted by the H1 type VI (H1-T6SS) secretion system that acts on bacterial target cells. The producing bacterium is protected by a cognate immunity protein.[1] [2] Publication Abstract from PubMedBacterial 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 A 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. Structural and functional insights into the delivery of a bacterial Rhs pore-forming toxin to the membrane.,Gonzalez-Magana A, Tascon I, Altuna-Alvarez J, Queralt-Martin M, Colautti J, Velazquez C, Zabala M, Rojas-Palomino J, Cardenas M, Alcaraz A, Whitney JC, Ubarretxena-Belandia I, Albesa-Jove D Nat Commun. 2023 Nov 28;14(1):7808. doi: 10.1038/s41467-023-43585-5. PMID:38016939[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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