Cryo-EM structures of an insecticidal Bt toxin reveal its mechanism of action on the membrane

The Vip3 family proteins from Bacillus thuringiensis are thought to exert their insecticidal activity through pore formation. Here authors present cryo-EM structures of a Vip3 family toxin in both inactive and activated forms and show the activated Vip3Bc1 in its pore forming conformation on the mem...

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Autores principales:	Matthew J. Byrne, Matthew G. Iadanza, Marcos Arribas Perez, Daniel P. Maskell, Rachel M. George, Emma L. Hesketh, Paul A. Beales, Marc D. Zack, Colin Berry, Rebecca F. Thompson
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/0bb0dfee8a6a4093bdf5ddddce351782
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spelling	oai:doaj.org-article:0bb0dfee8a6a4093bdf5ddddce3517822021-12-02T16:50:30ZCryo-EM structures of an insecticidal Bt toxin reveal its mechanism of action on the membrane10.1038/s41467-021-23146-42041-1723https://doaj.org/article/0bb0dfee8a6a4093bdf5ddddce3517822021-05-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-23146-4https://doaj.org/toc/2041-1723The Vip3 family proteins from Bacillus thuringiensis are thought to exert their insecticidal activity through pore formation. Here authors present cryo-EM structures of a Vip3 family toxin in both inactive and activated forms and show the activated Vip3Bc1 in its pore forming conformation on the membrane.Matthew J. ByrneMatthew G. IadanzaMarcos Arribas PerezDaniel P. MaskellRachel M. GeorgeEmma L. HeskethPaul A. BealesMarc D. ZackColin BerryRebecca F. ThompsonNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-9 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Matthew J. Byrne Matthew G. Iadanza Marcos Arribas Perez Daniel P. Maskell Rachel M. George Emma L. Hesketh Paul A. Beales Marc D. Zack Colin Berry Rebecca F. Thompson Cryo-EM structures of an insecticidal Bt toxin reveal its mechanism of action on the membrane
description	The Vip3 family proteins from Bacillus thuringiensis are thought to exert their insecticidal activity through pore formation. Here authors present cryo-EM structures of a Vip3 family toxin in both inactive and activated forms and show the activated Vip3Bc1 in its pore forming conformation on the membrane.
format	article
author	Matthew J. Byrne Matthew G. Iadanza Marcos Arribas Perez Daniel P. Maskell Rachel M. George Emma L. Hesketh Paul A. Beales Marc D. Zack Colin Berry Rebecca F. Thompson
author_facet	Matthew J. Byrne Matthew G. Iadanza Marcos Arribas Perez Daniel P. Maskell Rachel M. George Emma L. Hesketh Paul A. Beales Marc D. Zack Colin Berry Rebecca F. Thompson
author_sort	Matthew J. Byrne
title	Cryo-EM structures of an insecticidal Bt toxin reveal its mechanism of action on the membrane
title_short	Cryo-EM structures of an insecticidal Bt toxin reveal its mechanism of action on the membrane
title_full	Cryo-EM structures of an insecticidal Bt toxin reveal its mechanism of action on the membrane
title_fullStr	Cryo-EM structures of an insecticidal Bt toxin reveal its mechanism of action on the membrane
title_full_unstemmed	Cryo-EM structures of an insecticidal Bt toxin reveal its mechanism of action on the membrane
title_sort	cryo-em structures of an insecticidal bt toxin reveal its mechanism of action on the membrane
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/0bb0dfee8a6a4093bdf5ddddce351782
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Cryo-EM structures of an insecticidal Bt toxin reveal its mechanism of action on the membrane

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