5JZH

Cryo-EM structure of aerolysin prepore

5JZH の概要

• エントリーDOI: 10.2210/pdb5jzh/pdb
• EMDBエントリー: 8185
• 分子名称: Aerolysin (1 entity in total)
• 機能のキーワード: pore forming toxin, concentric beta-barrel, aerolysin, toxin
• 由来する生物種: Aeromonas hydrophila
• タンパク質・核酸の鎖数: 14
• 化学式量合計: 659106.43

構造登録者

Iacovache, I.,Zuber, B. (登録日: 2016-05-16, 公開日: 2016-07-13, 最終更新日: 2024-10-23)

主引用文献

Iacovache, I.,De Carlo, S.,Cirauqui, N.,Dal Peraro, M.,van der Goot, F.G.,Zuber, B.
Cryo-EM structure of aerolysin variants reveals a novel protein fold and the pore-formation process.
Nat Commun, 7:12062-12062, 2016

PubMed Abstract: Owing to their pathogenical role and unique ability to exist both as soluble proteins and transmembrane complexes, pore-forming toxins (PFTs) have been a focus of microbiologists and structural biologists for decades. PFTs are generally secreted as water-soluble monomers and subsequently bind the membrane of target cells. Then, they assemble into circular oligomers, which undergo conformational changes that allow membrane insertion leading to pore formation and potentially cell death. Aerolysin, produced by the human pathogen Aeromonas hydrophila, is the founding member of a major PFT family found throughout all kingdoms of life. We report cryo-electron microscopy structures of three conformational intermediates and of the final aerolysin pore, jointly providing insight into the conformational changes that allow pore formation. Moreover, the structures reveal a protein fold consisting of two concentric β-barrels, tightly kept together by hydrophobic interactions. This fold suggests a basis for the prion-like ultrastability of aerolysin pore and its stoichiometry.

PubMed: 27405240
DOI: 10.1038/ncomms12062

実験手法

ELECTRON MICROSCOPY (3.9 Å)