Cryo-EM structure of aerolysin variants reveals a novel protein fold and the pore-formation process
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Cryo-EM structure of aerolysin variants reveals a novel protein fold and the pore-formation process
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...
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Various aerolysin-like pore-forming proteins have been identified from bacteria to vertebrates. However, the mechanism of receptor recognition and/or pore formation of the eukaryotic members remains unknown. Here, we present the first crystal and electron microscopy structures of a vertebrate aerolysin-like protein from Danio rerio, termed Dln1, before and after pore formation. Each subunit of ...
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ژورنال
عنوان ژورنال: Nature Communications
سال: 2016
ISSN: 2041-1723
DOI: 10.1038/ncomms12062