Conformational Flexibility Is a Key Determinant for the Lytic Activity of the Pore-Forming Protein, Cytolysin A
Author:
Affiliation:
1. Department of Chemical Engineering, Indian Institute of Science, Bangalore, Karnataka 560012, India
2. Center for BioSystems Science and Engineering, Indian Institute of Science, Bangalore, Karnataka 560012, India
Publisher
American Chemical Society (ACS)
Subject
Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.jpcb.2c05785
Reference56 articles.
1. Pathogenic Pore-Forming Proteins: Function and Host Response
2. Pore-forming toxins: ancient, but never really out of fashion
3. The structure of a cytolytic α-helical toxin pore reveals its assembly mechanism
4. Molecular analysis of the cytolytic protein ClyA (SheA) from Escherichia coli
5. Capturing the Membrane-Triggered Conformational Transition of an α-Helical Pore-Forming Toxin
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