6GY6

XaxAB pore complex from Xenorhabdus nematophila

6GY6 の概要

• エントリーDOI: 10.2210/pdb6gy6/pdb
• EMDBエントリー: 0088
• 分子名称: XaxA, XaxB (2 entities in total)
• 機能のキーワード: bacterial toxin, pore forming-toxins, toxin
• 由来する生物種: Xenorhabdus nematophila ATCC 19061; 詳細
• タンパク質・核酸の鎖数: 26
• 化学式量合計: 1117799.11

構造登録者

Schubert, E.,Raunser, S. (登録日: 2018-06-28, 公開日: 2018-07-25, 最終更新日: 2024-11-13)

主引用文献

Schubert, E.,Vetter, I.R.,Prumbaum, D.,Penczek, P.A.,Raunser, S.
Membrane insertion of alpha-xenorhabdolysin in near-atomic detail.
Elife, 7:-, 2018

PubMed Abstract: α-Xenorhabdolysins (Xax) are α-pore-forming toxins (α-PFT) that form 1-1.3 MDa large pore complexes to perforate the host cell membrane. PFTs are used by a variety of bacterial pathogens to attack host cells. Due to the lack of structural information, the molecular mechanism of action of Xax toxins is poorly understood. Here, we report the cryo-EM structure of the XaxAB pore complex from and the crystal structures of the soluble monomers of XaxA and XaxB. The structures reveal that XaxA and XaxB are built similarly and appear as heterodimers in the 12-15 subunits containing pore, classifying XaxAB as bi-component α-PFT. Major conformational changes in XaxB, including the swinging out of an amphipathic helix are responsible for membrane insertion. XaxA acts as an activator and stabilizer for XaxB that forms the actual transmembrane pore. Based on our results, we propose a novel structural model for the mechanism of Xax intoxication.

PubMed: 30010541
DOI: 10.7554/eLife.38017

実験手法

ELECTRON MICROSCOPY (4 Å)