Cryo-EM structure of aerolysin variants reveals a novel protein fold and the pore-formation process

Aerolysin is a secreted bacterial pore forming toxin that inserts into the host plasma membrane, potentially leading to cell death. Here the authors present Cryo-EM structures of aerolysin arrested at different stages of the pore formation process that provide insight into the conformational changes...

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Autores principales:	Ioan Iacovache, Sacha De Carlo, Nuria Cirauqui, Matteo Dal Peraro, F. Gisou van der Goot, Benoît Zuber
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2016
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/cf673eee03eb4a2b9b6bf3aad1ad1011
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spelling	oai:doaj.org-article:cf673eee03eb4a2b9b6bf3aad1ad10112021-12-02T17:33:20ZCryo-EM structure of aerolysin variants reveals a novel protein fold and the pore-formation process10.1038/ncomms120622041-1723https://doaj.org/article/cf673eee03eb4a2b9b6bf3aad1ad10112016-07-01T00:00:00Zhttps://doi.org/10.1038/ncomms12062https://doaj.org/toc/2041-1723Aerolysin is a secreted bacterial pore forming toxin that inserts into the host plasma membrane, potentially leading to cell death. Here the authors present Cryo-EM structures of aerolysin arrested at different stages of the pore formation process that provide insight into the conformational changes that allow pore formation.Ioan IacovacheSacha De CarloNuria CirauquiMatteo Dal PeraroF. Gisou van der GootBenoît ZuberNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-8 (2016)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Ioan Iacovache Sacha De Carlo Nuria Cirauqui Matteo Dal Peraro F. Gisou van der Goot Benoît Zuber Cryo-EM structure of aerolysin variants reveals a novel protein fold and the pore-formation process
description	Aerolysin is a secreted bacterial pore forming toxin that inserts into the host plasma membrane, potentially leading to cell death. Here the authors present Cryo-EM structures of aerolysin arrested at different stages of the pore formation process that provide insight into the conformational changes that allow pore formation.
format	article
author	Ioan Iacovache Sacha De Carlo Nuria Cirauqui Matteo Dal Peraro F. Gisou van der Goot Benoît Zuber
author_facet	Ioan Iacovache Sacha De Carlo Nuria Cirauqui Matteo Dal Peraro F. Gisou van der Goot Benoît Zuber
author_sort	Ioan Iacovache
title	Cryo-EM structure of aerolysin variants reveals a novel protein fold and the pore-formation process
title_short	Cryo-EM structure of aerolysin variants reveals a novel protein fold and the pore-formation process
title_full	Cryo-EM structure of aerolysin variants reveals a novel protein fold and the pore-formation process
title_fullStr	Cryo-EM structure of aerolysin variants reveals a novel protein fold and the pore-formation process
title_full_unstemmed	Cryo-EM structure of aerolysin variants reveals a novel protein fold and the pore-formation process
title_sort	cryo-em structure of aerolysin variants reveals a novel protein fold and the pore-formation process
publisher	Nature Portfolio
publishDate	2016
url	https://doaj.org/article/cf673eee03eb4a2b9b6bf3aad1ad1011
work_keys_str_mv	AT ioaniacovache cryoemstructureofaerolysinvariantsrevealsanovelproteinfoldandtheporeformationprocess AT sachadecarlo cryoemstructureofaerolysinvariantsrevealsanovelproteinfoldandtheporeformationprocess AT nuriacirauqui cryoemstructureofaerolysinvariantsrevealsanovelproteinfoldandtheporeformationprocess AT matteodalperaro cryoemstructureofaerolysinvariantsrevealsanovelproteinfoldandtheporeformationprocess AT fgisouvandergoot cryoemstructureofaerolysinvariantsrevealsanovelproteinfoldandtheporeformationprocess AT benoitzuber cryoemstructureofaerolysinvariantsrevealsanovelproteinfoldandtheporeformationprocess
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Cryo-EM structure of aerolysin variants reveals a novel protein fold and the pore-formation process

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