6VRA

Anthrax octamer prechannel bound to full-length edema factor

6VRA の概要

• エントリーDOI: 10.2210/pdb6vra/pdb
• 関連するPDBエントリー: 6VR9
• EMDBエントリー: 21365
• 分子名称: Protective antigen, Calmodulin-sensitive adenylate cyclase, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: translocase, anthrax toxin, protective antigen, edema factor, octamer
• 由来する生物種: Bacillus anthracis; 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 1017067.59

構造登録者

Zhou, K.,Hardenbrook, N.J.,Liu, S.,Cui, Y.X.,Krantz, B.A.,Zhou, Z.H. (登録日: 2020-02-07, 公開日: 2020-12-16, 最終更新日: 2024-03-06)

主引用文献

Zhou, K.,Liu, S.,Hardenbrook, N.J.,Cui, Y.,Krantz, B.A.,Zhou, Z.H.
Atomic Structures of Anthrax Prechannel Bound with Full-Length Lethal and Edema Factors.
Structure, 28:879-887.e3, 2020

PubMed Abstract: Pathogenesis of anthrax disease involves two cytotoxic enzymes-edema factor (EF) and lethal factor (LF)-which are individually recruited by the protective antigen heptamer (PA) or octamer (PA) prechannel and subsequently translocated across channels formed on the endosomal membrane upon exposure to low pH. Here, we report the atomic structures of PA prechannel-bound full-length EF and LF. In this pretranslocation state, the N-terminal segment of both factors refolds into an α helix engaged in the α clamp of the prechannel. Recruitment to the PA prechannel exposes an originally buried β strand of both toxins and enables domain organization of EF. Many interactions occur on domain interfaces in both PA prechannel-bound EF and LF, leading to toxin compaction prior to translocation. Our results provide key insights into the molecular mechanisms of translocation-coupled protein unfolding and translocation.

PubMed: 32521227
DOI: 10.1016/j.str.2020.05.009

実験手法

ELECTRON MICROSCOPY (3.3 Å)