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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Main Authors:	Monika Bokori-Brown, Thomas G. Martin, Claire E. Naylor, Ajit K. Basak, Richard W. Titball, Christos G. Savva
Format:	Article
Language:	English
Published:	Nature Publishing Group 2016-04-01
Series:	Nature Communications
Online Access:	https://doi.org/10.1038/ncomms11293

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spelling	doaj-b12960b2d8de44f388f6f4d400e7f3cc2021-05-11T11:14:17ZengNature Publishing GroupNature Communications2041-17232016-04-01711710.1038/ncomms11293Cryo-EM structure of lysenin pore elucidates membrane insertion by an aerolysin family proteinMonika Bokori-Brown0Thomas G. Martin1Claire E. Naylor2Ajit K. Basak3Richard W. Titball4Christos G. Savva5Biosciences, College of Life and Environmental Sciences, University of ExeterMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge Biomedical CampusDepartment of Biological Sciences, Birkbeck CollegeDepartment of Biological Sciences, Birkbeck CollegeBiosciences, College of Life and Environmental Sciences, University of ExeterMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge Biomedical CampusLysenin 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.https://doi.org/10.1038/ncomms11293
collection	DOAJ
language	English
format	Article
sources	DOAJ
author	Monika Bokori-Brown Thomas G. Martin Claire E. Naylor Ajit K. Basak Richard W. Titball Christos G. Savva
spellingShingle	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 Nature Communications
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 Publishing Group
series	Nature Communications
issn	2041-1723
publishDate	2016-04-01
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.
url	https://doi.org/10.1038/ncomms11293
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Cryo-EM structure of lysenin pore elucidates membrane insertion by an aerolysin family protein

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