Involvement of domain 3 in oligomerization by the protective antigen moiety of anthrax toxin |
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Authors: | Mogridge J Mourez M Collier R J |
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Institution: | Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Massachusetts 02115, USA. |
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Abstract: | Protective antigen (PA), a component of anthrax toxin, binds receptors on mammalian cells and is activated by a cell surface protease. The resulting active fragment, PA(63), forms ring-shaped heptamers, binds the enzymic moieties of the toxin, and translocates them to the cytosol. Of the four crystallographic domains of PA, domain 1 has been implicated in binding the enzymic moieties; domain 2 is involved in membrane insertion and oligomerization; and domain 4 binds receptor. To determine the function of domain 3, we developed a screen that allowed us to isolate random mutations that cause defects in the activity of PA. We identified several mutations in domain 3 that affect monomer-monomer interactions in the PA(63) heptamer, indicating that this may be the primary function of this domain. |
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