Crystal structure of an invertebrate cytolysin pore reveals unique properties and mechanism of assembly

Crystal structure of an invertebrate cytolysin pore reveals unique properties and mechanism of assembly

Pore-forming toxins act by forming oligomeric pores in lipid membranes. Here the authors report the crystal structure of the lysenin pore, providing insights into the assembly and function of the pore in addition to suggesting that its properties make lysenin potentially well-suited for nanopore sen...

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Bibliographic Details
Main Authors: Marjetka Podobnik, Peter Savory, Nejc Rojko, Matic Kisovec, Neil Wood, Richard Hambley, Jonathan Pugh, E. Jayne Wallace, Luke McNeill, Mark Bruce, Idlir Liko, Timothy M. Allison, Shahid Mehmood, Neval Yilmaz, Toshihide Kobayashi, Robert J. C. Gilbert, Carol V. Robinson, Lakmal Jayasinghe, Gregor Anderluh
Format: Article
Language:English
Published: Nature Publishing Group 2016-05-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/ncomms11598

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https://doi.org/10.1038/ncomms11598

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