Cys−Cys Cross-Linking Shows Contact between the N-Terminus of Lethal Factor and Phe427 of the Anthrax Toxin Pore
Author:
Affiliation:
1. Department of Microbiology and Molecular Genetics, Harvard Medical School, 200 Longwood Ave., Boston, Massachusetts 02115, United States
Funder
National Institutes of Health
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi1017446
Reference23 articles.
1. The Protective Antigen Component of Anthrax Toxin Forms Functional Octameric Complexes
2. Stoichiometry of Anthrax Toxin Complexes
3. Anthrax Toxin: Receptor Binding, Internalization, Pore Formation, and Translocation
4. Mapping the Anthrax Protective Antigen Binding Site on the Lethal and Edema Factors
5. Crystal structure of the anthrax lethal factor
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1. Engineered Cross-Linking to Study the Pore Architecture of the CRAC Channel;The CRAC Channel;2018
2. Asymmetric Cryo-EM Structure of Anthrax Toxin Protective Antigen Pore with Lethal Factor N-Terminal Domain;Toxins;2017-09-22
3. Following Natures Lead: On the Construction of Membrane-Inserted Toxins in Lipid Bilayer Nanodiscs;The Journal of Membrane Biology;2015-01-13
4. NMR conformational properties of an Anthrax Lethal Factor domain studied by multiple amino acid-selective labeling;Biochemical and Biophysical Research Communications;2014-07
5. Secretory expression and efficient purification of recombinant anthrax toxin lethal factor with full biological activity in E. coli;Protein Expression and Purification;2013-05
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