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TitleCryo-EM structure of lysenin pore elucidates membrane insertion by an aerolysin family protein.
Journal, issue, pagesNat Commun, Vol. 7, Page 11293, Year 2016
Publish dateApr 6, 2016
AuthorsMonika Bokori-Brown / Thomas G Martin / Claire E Naylor / Ajit K Basak / Richard W Titball / Christos G Savva /
PubMed AbstractLysenin 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. ...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.
External linksNat Commun / PubMed:27048994 / PubMed Central
MethodsEM (single particle)
Resolution3.1 Å
Structure data

8015

5gaq

EMDB-8015, PDB-5gaq:
Cryo-EM structure of the Lysenin Pore
Method: EM (single particle) / Resolution: 3.1 Å

Source
  • Eisenia foetida (common brandling worm)
  • eisenia fetida (common brandling worm)
KeywordsTOXIN / Pore forming protein / aerolysin

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