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Publication Abstract from PubMed

Tripartite members of the ClyA family of alpha-PFTs have recently been identified in a number of pathogenic Gram-negative bacteria, including the human pathogen Serratia marcescens. Structures of a Gram-negative A component and a tripartite alpha-PFT complete pore are unknown and a mechanism for pore formation is still uncertain. Here we characterise the tripartite SmhABC toxin from S. marcescens and propose a mechanism of pore assembly. We present the structure of soluble SmhA, as well as the soluble and pore forms of SmhB. We show that the beta-tongue soluble structure is well conserved in the family and propose two conserved latches between the head and tail domains that are broken on the soluble to pore conformational change. Using the structures of individual components, sequence analysis and docking predictions we illustrate how the A, B and C protomers would assemble on the membrane to produce a complete tripartite alpha-PFT pore.

Characterisation of a tripartite alpha-pore forming toxin from Serratia marcescens.,Churchill-Angus AM, Schofield THB, Marlow TR, Sedelnikova SE, Wilson JS, Rafferty JB, Baker PJ Sci Rep. 2021 Mar 19;11(1):6447. doi: 10.1038/s41598-021-85726-0. PMID:33742033^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.