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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Autores principales: 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
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Publicado: Nature Portfolio 2016
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Acceso en línea:https://doaj.org/article/f5376f82acc44644923125077c3a3c57
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spelling oai:doaj.org-article:f5376f82acc44644923125077c3a3c572021-12-02T14:39:13ZCrystal structure of an invertebrate cytolysin pore reveals unique properties and mechanism of assembly10.1038/ncomms115982041-1723https://doaj.org/article/f5376f82acc44644923125077c3a3c572016-05-01T00:00:00Zhttps://doi.org/10.1038/ncomms11598https://doaj.org/toc/2041-1723Pore-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 sensing applications.Marjetka PodobnikPeter SavoryNejc RojkoMatic KisovecNeil WoodRichard HambleyJonathan PughE. Jayne WallaceLuke McNeillMark BruceIdlir LikoTimothy M. AllisonShahid MehmoodNeval YilmazToshihide KobayashiRobert J. C. GilbertCarol V. RobinsonLakmal JayasingheGregor AnderluhNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-10 (2016)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
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
Crystal structure of an invertebrate cytolysin pore reveals unique properties and mechanism of assembly
description 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 sensing applications.
format article
author 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
author_facet 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
author_sort Marjetka Podobnik
title Crystal structure of an invertebrate cytolysin pore reveals unique properties and mechanism of assembly
title_short Crystal structure of an invertebrate cytolysin pore reveals unique properties and mechanism of assembly
title_full Crystal structure of an invertebrate cytolysin pore reveals unique properties and mechanism of assembly
title_fullStr Crystal structure of an invertebrate cytolysin pore reveals unique properties and mechanism of assembly
title_full_unstemmed Crystal structure of an invertebrate cytolysin pore reveals unique properties and mechanism of assembly
title_sort crystal structure of an invertebrate cytolysin pore reveals unique properties and mechanism of assembly
publisher Nature Portfolio
publishDate 2016
url https://doaj.org/article/f5376f82acc44644923125077c3a3c57
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