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...
Main Authors: | , , , , , |
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Format: | Article |
Language: | English |
Published: |
Nature Publishing Group
2016-04-01
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Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/ncomms11293 |
Summary: | 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. |
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ISSN: | 2041-1723 |