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Significance Tc toxin complexes are virulence factors of many bacteria, including insect and human pathogens. Tc toxins are promising candidates for potential biopesticides as alternatives toBacillus thuringiensis toxins. We report 2 high-resolution cryo-EM structures of a Tc holotoxin embedded in the membrane. These structures, along with biochemical studies, contribute to our understanding of key steps of the prepore-to-pore transition, membrane insertion, and toxin translocation mechanisms of this biotechnologically relevant type of bacterial toxin. Our study provides important insights into the mechanism of action of Tc toxins and can serve as a strong foundation for the development of biopesticides.

Structure of a Tc holotoxin pore provides insights into the translocation mechanism