Structure of the Diphtheria Toxin at Acidic pH: Implications for the Conformational Switching of the Translocation Domain

Structure of the Diphtheria Toxin at Acidic pH: Implications for the Conformational Switching of the Translocation Domain

Diphtheria toxin, an exotoxin secreted by <i>Corynebacterium</i> that causes disease in humans by inhibiting protein synthesis, enters the cell via receptor-mediated endocytosis. The subsequent endosomal acidification triggers a series of conformational changes, resulting in the refoldin...

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Bibliographic Details
Main Authors: Mykola V. Rodnin, Maithri M. Kashipathy, Alexander Kyrychenko, Kevin P. Battaile, Scott Lovell, Alexey S. Ladokhin
Format: Article
Language:English
Published: MDPI AG 2020-11-01
Series:Toxins
Subjects:
diphtheria toxin structure
X-ray crystallography
helix unfolding
acidification
conformational switching
Online Access:https://www.mdpi.com/2072-6651/12/11/704

Internet

https://www.mdpi.com/2072-6651/12/11/704

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