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    Cryo-EM structure of lysenin pore elucidates membrane insertion by an aerolysin family protein

    Bokori-Brown, M. and Martin, T.G. and Naylor, Claire and Basak, Ajit K. and Titball, R.W. and Savva, Christos (2016) Cryo-EM structure of lysenin pore elucidates membrane insertion by an aerolysin family protein. Nature Communications 7 , p. 11293. ISSN 2041-1723.

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    Abstract

    Lysenin from the coelomic fluid of the earthworm Eisenia fetida belongs to the aerolysin family of small β-pore-forming toxins (β-PFTs), some members of which are pathogenic to humans and animals. Despite efforts, a high-resolution structure of a channel for this family of proteins has been elusive and therefore the mechanism of activation and membrane insertion remains unclear. Here we determine the pore structure of lysenin by single particle cryo-EM, to 3.1 Å resolution. The nonameric assembly reveals a long β-barrel channel spanning the length of the complex that, unexpectedly, includes the two pre-insertion strands flanking the hypothetical membrane-insertion loop. Examination of other members of the aerolysin family reveals high structural preservation in this region, indicating that the membrane-insertion pathway in this family is conserved. For some toxins, proteolytic activation and pro-peptide removal will facilitate unfolding of the pre-insertion strands, allowing them to form the β-barrel of the channel.

    Metadata

    Item Type: Article
    Keyword(s) / Subject(s): Biological sciences, Biophysics, Microbiology
    School: Birkbeck Schools and Departments > School of Science > Biological Sciences
    Depositing User: Administrator
    Date Deposited: 16 May 2016 14:33
    Last Modified: 27 Jul 2019 16:48
    URI: http://eprints.bbk.ac.uk/id/eprint/15183

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