Cryo-EM structure of lysenin pore elucidates membrane insertion by an aerolysin family protein

Lysenin is member of the aerolysin family of small ß-barrel pore-forming toxins that include virulence factors from several human and animal pathogens. Here the authors determine the structure of the lysenin pore by single particle cryo- EM and propose a conserved pore formation mechanism for the ae...

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Autores principales:	Monika Bokori-Brown, Thomas G. Martin, Claire E. Naylor, Ajit K. Basak, Richard W. Titball, Christos G. Savva
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2016
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/b12960b2d8de44f388f6f4d400e7f3cc
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spelling	oai:doaj.org-article:b12960b2d8de44f388f6f4d400e7f3cc2021-12-02T16:50:55ZCryo-EM structure of lysenin pore elucidates membrane insertion by an aerolysin family protein10.1038/ncomms112932041-1723https://doaj.org/article/b12960b2d8de44f388f6f4d400e7f3cc2016-04-01T00:00:00Zhttps://doi.org/10.1038/ncomms11293https://doaj.org/toc/2041-1723Lysenin is member of the aerolysin family of small ß-barrel pore-forming toxins that include virulence factors from several human and animal pathogens. Here the authors determine the structure of the lysenin pore by single particle cryo- EM and propose a conserved pore formation mechanism for the aerolysin protein family.Monika Bokori-BrownThomas G. MartinClaire E. NaylorAjit K. BasakRichard W. TitballChristos G. SavvaNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-7 (2016)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Monika Bokori-Brown Thomas G. Martin Claire E. Naylor Ajit K. Basak Richard W. Titball Christos G. Savva Cryo-EM structure of lysenin pore elucidates membrane insertion by an aerolysin family protein
description	Lysenin is member of the aerolysin family of small ß-barrel pore-forming toxins that include virulence factors from several human and animal pathogens. Here the authors determine the structure of the lysenin pore by single particle cryo- EM and propose a conserved pore formation mechanism for the aerolysin protein family.
format	article
author	Monika Bokori-Brown Thomas G. Martin Claire E. Naylor Ajit K. Basak Richard W. Titball Christos G. Savva
author_facet	Monika Bokori-Brown Thomas G. Martin Claire E. Naylor Ajit K. Basak Richard W. Titball Christos G. Savva
author_sort	Monika Bokori-Brown
title	Cryo-EM structure of lysenin pore elucidates membrane insertion by an aerolysin family protein
title_short	Cryo-EM structure of lysenin pore elucidates membrane insertion by an aerolysin family protein
title_full	Cryo-EM structure of lysenin pore elucidates membrane insertion by an aerolysin family protein
title_fullStr	Cryo-EM structure of lysenin pore elucidates membrane insertion by an aerolysin family protein
title_full_unstemmed	Cryo-EM structure of lysenin pore elucidates membrane insertion by an aerolysin family protein
title_sort	cryo-em structure of lysenin pore elucidates membrane insertion by an aerolysin family protein
publisher	Nature Portfolio
publishDate	2016
url	https://doaj.org/article/b12960b2d8de44f388f6f4d400e7f3cc
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Cryo-EM structure of lysenin pore elucidates membrane insertion by an aerolysin family protein

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