7a26

Structure of soluble SmhA crystal form 1 of the tripartite alpha-pore forming toxin, Smh, from Serratia marcescens.

spinqualitylabelsall models 7a26, resolution 2.98Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.98Å Ligands: CA, CL, MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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