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Toxins 2018, 10(9), 343;

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

Center for Integrated Protein Science Munich (CIPSM), Department of Chemistry, Technische Universität München, Lichtenbergstrasse 4, 85747 Garching, Germany
Authors to whom correspondence should be addressed.
Received: 27 July 2018 / Revised: 16 August 2018 / Accepted: 22 August 2018 / Published: 23 August 2018
(This article belongs to the Special Issue Bacterial Toxins: Structure–Function Relationship)
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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. View Full-Text
Keywords: pore-forming toxins (PFT); virulence factors; structural biology; x-ray crystallography; cryo-electron microscopy pore-forming toxins (PFT); virulence factors; structural biology; x-ray crystallography; cryo-electron microscopy

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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

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Bräuning, B.; Groll, M. Structural and Mechanistic Features of ClyA-Like α-Pore-Forming Toxins. Toxins 2018, 10, 343.

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