7A0G

Structure of the SmhB pore of the tripartite alpha-pore forming toxin, Smh, from Serratia marcescens.

これはPDB形式変換不可エントリーです。

7A0G の概要

• エントリーDOI: 10.2210/pdb7a0g/pdb
• 分子名称: SmhB (1 entity in total)
• 機能のキーワード: pore, pore forming toxin, toxin, bacterial toxin, serratia marcescens
• 由来する生物種: Serratia marcescens
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 393765.62

構造登録者

Churchill-Angus, A.M.,Baker, P.J. (登録日: 2020-08-08, 公開日: 2021-03-31, 最終更新日: 2024-01-31)

主引用文献

Churchill-Angus, A.M.,Schofield, T.H.B.,Marlow, T.R.,Sedelnikova, S.E.,Wilson, J.S.,Rafferty, J.B.,Baker, P.J.
Characterisation of a tripartite alpha-pore forming toxin from Serratia marcescens
Sci Rep, 11:6447-, 2021

PubMed Abstract: Tripartite members of the ClyA family of α-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 α-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 β-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 α-PFT pore.

PubMed: 33742033
DOI: 10.1038/s41598-021-85726-0

実験手法

X-RAY DIFFRACTION (6.979 Å)