6RB9

The pore structure of Clostridium perfringens epsilon toxin

6RB9 の概要

• エントリーDOI: 10.2210/pdb6rb9/pdb
• EMDBエントリー: 4789
• 分子名称: Epsilon-toxin type B (1 entity in total)
• 機能のキーワード: enterotoxaemia, beta-pft, epsilon toxin, cryoem, toxin
• 由来する生物種: Clostridium perfringens B
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 225642.86

構造登録者

Savva, C.G.,Clark, A.R.,Naylor, C.E.,Popoff, M.R.,Moss, D.S.,Basak, A.K.,Titball, R.W.,Bokori-Brown, M. (登録日: 2019-04-09, 公開日: 2019-06-19, 最終更新日: 2024-05-22)

主引用文献

Savva, C.G.,Clark, A.R.,Naylor, C.E.,Popoff, M.R.,Moss, D.S.,Basak, A.K.,Titball, R.W.,Bokori-Brown, M.
The pore structure of Clostridium perfringens epsilon toxin.
Nat Commun, 10:2641-2641, 2019

PubMed Abstract: Epsilon toxin (Etx), a potent pore forming toxin (PFT) produced by Clostridium perfringens, is responsible for the pathogenesis of enterotoxaemia of ruminants and has been suggested to play a role in multiple sclerosis in humans. Etx is a member of the aerolysin family of β-PFTs (aβ-PFTs). While the Etx soluble monomer structure was solved in 2004, Etx pore structure has remained elusive due to the difficulty of isolating the pore complex. Here we show the cryo-electron microscopy structure of Etx pore assembled on the membrane of susceptible cells. The pore structure explains important mutant phenotypes and suggests that the double β-barrel, a common feature of the aβ-PFTs, may be an important structural element in driving efficient pore formation. These insights provide the framework for the development of novel therapeutics to prevent human and animal infections, and are relevant for nano-biotechnology applications.

PubMed: 31201325
DOI: 10.1038/s41467-019-10645-8

実験手法

ELECTRON MICROSCOPY (3.2 Å)