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: | 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 |
Similar Items
-
Elucidation of the mode of action of the pore-forming toxin aerolysin on T lymphomas
by: Nelson, Kimberlea Lynne
Published: (2018) -
The pore structure of Clostridium perfringens epsilon toxin
by: Christos G. Savva, et al.
Published: (2019-06-01) -
Temporary Membrane Permeabilization via the Pore-Forming Toxin Lysenin
by: Nisha Shrestha, et al.
Published: (2020-05-01) -
Identification of a Key Residue for Oligomerisation and Pore-Formation of Clostridium perfringens NetB
by: Sérgio P. Fernandes da Costa, et al.
Published: (2014-03-01) -
Cryo-EM structure of aerolysin variants reveals a novel protein fold and the pore-formation process
by: Ioan Iacovache, et al.
Published: (2016-07-01)