+検索条件
-Structure paper
タイトル | Common architecture of Tc toxins from human and insect pathogenic bacteria. |
---|---|
ジャーナル・号・ページ | Sci Adv, Vol. 5, Issue 10, Page eaax6497, Year 2019 |
掲載日 | 2019年10月16日 |
著者 | F Leidreiter / D Roderer / D Meusch / C Gatsogiannis / R Benz / S Raunser / |
PubMed 要旨 | 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. |
リンク | Sci Adv / PubMed:31663026 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 2.75 - 4.0 Å |
構造データ | EMDB-10033, PDB-6rw6: EMDB-10034, PDB-6rw8: EMDB-10035, PDB-6rw9: EMDB-10036, PDB-6rwa: EMDB-10037, PDB-6rwb: |
由来 |
|
キーワード | TOXIN / membrane permeation / translocation / complex |