Anthrax toxin translocation complex reveals insight into the lethal factor unfolding and refolding mechanism.

ABSTRACT: Translocation is essential to the anthrax toxin mechanism. Protective antigen (PA), the binding component of this AB toxin, forms an oligomeric pore that translocates lethal factor (LF) or edema factor, the active components of the toxin, into the cell. Structural details of the translocation process have remained elusive despite their biological importance. To overcome the technical challenges of studying translocation intermediates, we developed a method to immobilize, transition, and stabilize anthrax toxin to mimic important physiological steps in the intoxication process. Here, we report a cryoEM snapshot of PA_pore translocating the N-terminal domain of LF (LF_N). The resulting 3.3 Å structure of the complex shows density of partially unfolded LF_N near

SUBMITTER: Machen AJ 

PROVIDER: S-EPMC8219829 | biostudies-literature | 2021 Jun

REPOSITORIES: biostudies-literature