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-Structure paper
| Title | Common architecture of Tc toxins from human and insect pathogenic bacteria. |
|---|---|
| Journal, issue, pages | Sci Adv, Vol. 5, Issue 10, Page eaax6497, Year 2019 |
| Publish date | Oct 16, 2019 |
 Authors | F Leidreiter / D Roderer / D Meusch / C Gatsogiannis / R Benz / S Raunser /  |
| PubMed Abstract | Tc toxins use a syringe-like mechanism to penetrate the membrane and translocate toxic enzymes into the host cytosol. They are composed of three components: TcA, TcB, and TcC. Low-resolution ...Tc toxins use a syringe-like mechanism to penetrate the membrane and translocate toxic enzymes into the host cytosol. They are composed of three components: TcA, TcB, and TcC. Low-resolution structures of TcAs from different bacteria suggest a considerable difference in their architecture and possibly in their mechanism of action. Here, we present high-resolution structures of five TcAs from insect and human pathogens, which show a similar overall composition and domain organization. Essential structural features, including a trefoil protein knot, are present in all TcAs, suggesting a common mechanism of action. All TcAs form functional pores and can be combined with TcB-TcC subunits from other species to form active chimeric holotoxins. We identified a conserved ionic pair that stabilizes the shell, likely operating as a strong latch that only springs open after destabilization of other regions. Our results provide new insights into the architecture and mechanism of the Tc toxin family. |
 External links | Sci Adv / PubMed:31663026 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 2.75 - 4.0 Å |
| Structure data | EMDB-10033, PDB-6rw6: EMDB-10034, PDB-6rw8: EMDB-10035, PDB-6rw9: EMDB-10036, PDB-6rwa: EMDB-10037, PDB-6rwb: |
| Source |
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 Keywords |  TOXIN / membrane permeation / translocation / complex |
