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Lysenin is a PFT of Eisena fetida and a member of the aerolysin family. It is a nonamer and forms an 18-strand smooth-walled tubular ß barrel attached to the outside by the C-terminal domains. It is a mushroom-like structure which has a transmembrane pore with a central stem built of a long ß barrel. Having a uniform and stable ß barrel through the entire length of protein makes lysenin an exception among PFTs.
Crystal structure of an invertebrate cytolysin pore reveals unique properties and mechanism of assembly
Nat Commun. 2016 May 12;7:11598. doi: 10.1038/ncomms11598.
Cryo-EM structure of lysenin pore elucidates membrane insertion by an aerolysin family protein
Nat Commun. 2016 Apr 6;7:11293. doi: 10.1038/ncomms11293.
A role for sphingomyelin-rich lipid domains in the accumulation of phosphatidylinositol-4,5-bisphosphate to the cleavage furrow during cytokinesis
Mol Cell Biol. 2012 Apr;32(8):1396-407. doi: 10.1128/MCB.06113-11. Epub 2012 Feb 13.