8CP6

Type six secretion system exported effector 5 (Tse5)

Summary for 8CP6

• Entry DOI: 10.2210/pdb8cp6/pdb
• EMDB information: 16778
• Descriptor: Toxin protein Tse5 (3 entities in total)
• Functional Keywords: pore-forming protein, p.aeruginosa, effector, bacterial rearrangement hot spot protein, ion channel, type vi secretion system, toxin
• Biological source: Pseudomonas aeruginosa; More
• Total number of polymer chains: 3
• Total formula weight: 149018.79

Authors

Gonzalez-Magana, A.,Tascon, I.,Ubarretxena-Belandia, I.,Albesa-Jove, D. (deposition date: 2023-03-01, release date: 2023-12-06)

Primary citation

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, J.C.,Ubarretxena-Belandia, I.,Albesa-Jove, D.
Structural and functional insights into the delivery of a bacterial Rhs pore-forming toxin to the membrane.
Nat Commun, 14:7808-7808, 2023

PubMed Abstract: 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.

PubMed: 38016939
DOI: 10.1038/s41467-023-43585-5

Experimental method

ELECTRON MICROSCOPY (2.45 Å)