Cargando…
Cryo-EM structure of lysenin pore elucidates membrane insertion by an aerolysin family protein
Lysenin from the coelomic fluid of the earthworm Eisenia fetida belongs to the aerolysin family of small β-pore-forming toxins (β-PFTs), some members of which are pathogenic to humans and animals. Despite efforts, a high-resolution structure of a channel for this family of proteins has been elusive...
Autores principales: | Bokori-Brown, Monika, Martin, Thomas G., Naylor, Claire E., Basak, Ajit K., Titball, Richard W., Savva, Christos G. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2016
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4823867/ https://www.ncbi.nlm.nih.gov/pubmed/27048994 http://dx.doi.org/10.1038/ncomms11293 |
Ejemplares similares
-
The pore structure of Clostridium perfringens epsilon toxin
por: Savva, Christos G., et al.
Publicado: (2019) -
Identification of a Key Residue for Oligomerisation and Pore-Formation of Clostridium perfringens NetB
por: Fernandes da Costa, Sérgio P., et al.
Publicado: (2014) -
Molecular Architecture and Functional Analysis of NetB, a Pore-forming Toxin from Clostridium perfringens
por: Savva, Christos G., et al.
Publicado: (2013) -
Cryo-EM structure of aerolysin variants reveals a novel protein fold and the pore-formation process
por: Iacovache, Ioan, et al.
Publicado: (2016) -
Clostridium perfringens epsilon toxin H149A mutant as a platform for receptor binding studies
por: Bokori-Brown, Monika, et al.
Publicado: (2013)