dc.contributor.author | Bokori-Brown, M | |
dc.contributor.author | Martin, TG | |
dc.contributor.author | Naylor, CE | |
dc.contributor.author | Basak, AK | |
dc.contributor.author | Titball, RW | |
dc.contributor.author | Savva, CG | |
dc.date.accessioned | 2016-06-10T09:12:56Z | |
dc.date.issued | 2016-04-06 | |
dc.description.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. | en_GB |
dc.description.sponsorship | This work was supported by grants from the UK Medical Research Council (MC-A021-53019) and the Wellcome Trust (WT089618MA) | en_GB |
dc.identifier.citation | Vol. 7, article 11293 | en_GB |
dc.identifier.doi | 10.1038/ncomms11293 | |
dc.identifier.uri | http://hdl.handle.net/10871/21968 | |
dc.language.iso | en | en_GB |
dc.publisher | Springer Nature | en_GB |
dc.relation.url | http://www.ncbi.nlm.nih.gov/pubmed/27048994 | en_GB |
dc.rights | Open access. This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ | en_GB |
dc.subject | Biological sciences | en_GB |
dc.subject | Biophysics | en_GB |
dc.subject | Microbiology | en_GB |
dc.title | Cryo-EM structure of lysenin pore elucidates membrane insertion by an aerolysin family protein | en_GB |
dc.type | Article | en_GB |
dc.date.available | 2016-06-10T09:12:56Z | |
exeter.place-of-publication | England | |
dc.description | This is the final version of the article. Available from Springer Nature via the DOI in this record. | en_GB |
dc.identifier.journal | Nature Communications | en_GB |