6RWB
Cryo-EM structure of Yersinia pseudotuberculosis TcaA-TcaB
Summary for 6RWB
| Entry DOI | 10.2210/pdb6rwb/pdb |
| Related | 6RW6 6RW8 6RW9 6RWA |
| EMDB information | 10037 |
| Descriptor | Toxin,Toxin complex subunit TcaB,Putative toxin subunit,Putative toxin subunit,Toxin,Toxin complex subunit TcaB,Putative toxin subunit,Putative toxin subunit,Toxin,Toxin complex subunit TcaB,Putative toxin subunit,Putative toxin subunit,Toxin,Toxin complex subunit TcaB,Putative toxin subunit,Putative toxin subunit (1 entity in total) |
| Functional Keywords | toxin, membrane permeation, translocation, complex |
| Biological source | Yersinia pseudotuberculosis More |
| Total number of polymer chains | 5 |
| Total formula weight | 1159925.16 |
| Authors | Roderer, D.,Leidreiter, F.,Gatsogiannis, C.,Meusch, D.,Benz, R.,Raunser, S. (deposition date: 2019-06-04, release date: 2019-10-23, Last modification date: 2024-05-22) |
| Primary citation | Leidreiter, F.,Roderer, D.,Meusch, D.,Gatsogiannis, C.,Benz, R.,Raunser, S. Common architecture of Tc toxins from human and insect pathogenic bacteria. Sci Adv, 5:eaax6497-eaax6497, 2019 Cited by 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 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. PubMed: 31663026DOI: 10.1126/sciadv.aax6497 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.25 Å) |
Structure validation
Download full validation report
