5JZW

Cryo-EM structures of aerolysin post-prepore and quasipore

Summary for 5JZW

• Entry DOI: 10.2210/pdb5jzw/pdb
• EMDB information: 8188
• Descriptor: Aerolysin (1 entity in total)
• Functional Keywords: pore forming toxin, concentric beta-barrel, aerolysin, toxin
• Biological source: Aeromonas hydrophila
• Total number of polymer chains: 14
• Total formula weight: 659864.03

Authors

Iacovache, I.,Zuber, B. (deposition date: 2016-05-17, release date: 2016-07-13, Last modification date: 2018-11-21)

Primary citation

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

Experimental method

ELECTRON MICROSCOPY (4.46 Å)