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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...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2018
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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. |
format | Online Article Text |
id | pubmed-6162564 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
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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