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Structural and Mechanistic Features of ClyA-Like α-Pore-Forming Toxins

Recent technological advances have seen increasing numbers of complex structures from diverse pore-forming toxins (PFT). The ClyA family of α-PFTs comprises a broad variety of assemblies including single-, two- and three-component toxin systems. With crystal structures available for soluble subunits...

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Autores principales: Bräuning, Bastian, Groll, Michael
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6162564/
https://www.ncbi.nlm.nih.gov/pubmed/30142951
http://dx.doi.org/10.3390/toxins10090343
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author Bräuning, Bastian
Groll, Michael
author_facet Bräuning, Bastian
Groll, Michael
author_sort Bräuning, Bastian
collection PubMed
description Recent technological advances have seen increasing numbers of complex structures from diverse pore-forming toxins (PFT). The ClyA family of α-PFTs comprises a broad variety of assemblies including single-, two- and three-component toxin systems. With crystal structures available for soluble subunits of all major groups in this extended protein family, efforts now focus on obtaining molecular insights into physiological pore formation. This review provides an up-to-date discussion on common and divergent structural and functional traits that distinguish the various ClyA family PFTs. Open questions of this research topic are outlined and discussed.
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spelling pubmed-61625642018-10-03 Structural and Mechanistic Features of ClyA-Like α-Pore-Forming Toxins Bräuning, Bastian Groll, Michael Toxins (Basel) Review Recent technological advances have seen increasing numbers of complex structures from diverse pore-forming toxins (PFT). The ClyA family of α-PFTs comprises a broad variety of assemblies including single-, two- and three-component toxin systems. With crystal structures available for soluble subunits of all major groups in this extended protein family, efforts now focus on obtaining molecular insights into physiological pore formation. This review provides an up-to-date discussion on common and divergent structural and functional traits that distinguish the various ClyA family PFTs. Open questions of this research topic are outlined and discussed. MDPI 2018-08-23 /pmc/articles/PMC6162564/ /pubmed/30142951 http://dx.doi.org/10.3390/toxins10090343 Text en © 2018 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Bräuning, Bastian
Groll, Michael
Structural and Mechanistic Features of ClyA-Like α-Pore-Forming Toxins
title Structural and Mechanistic Features of ClyA-Like α-Pore-Forming Toxins
title_full Structural and Mechanistic Features of ClyA-Like α-Pore-Forming Toxins
title_fullStr Structural and Mechanistic Features of ClyA-Like α-Pore-Forming Toxins
title_full_unstemmed Structural and Mechanistic Features of ClyA-Like α-Pore-Forming Toxins
title_short Structural and Mechanistic Features of ClyA-Like α-Pore-Forming Toxins
title_sort structural and mechanistic features of clya-like α-pore-forming toxins
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6162564/
https://www.ncbi.nlm.nih.gov/pubmed/30142951
http://dx.doi.org/10.3390/toxins10090343
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