7Q9Y
Cryo-EM structure of the octameric pore of Clostridium perfringens beta-toxin.
Summary for 7Q9Y
Entry DOI | 10.2210/pdb7q9y/pdb |
EMDB information | 13876 |
Descriptor | Clostridium perfringens beta toxin (1 entity in total) |
Functional Keywords | pore forming toxin, hemolysin, octamer, toxin |
Biological source | Clostridium perfringens CPE |
Total number of polymer chains | 8 |
Total formula weight | 279150.00 |
Authors | Iacovache, I.,Zuber, B. (deposition date: 2021-11-15, release date: 2022-10-19, Last modification date: 2024-07-17) |
Primary citation | Bruggisser, J.,Iacovache, I.,Musson, S.C.,Degiacomi, M.T.,Posthaus, H.,Zuber, B. Cryo-EM structure of the octameric pore of Clostridium perfringens beta-toxin. Embo Rep., 23:e54856-e54856, 2022 Cited by PubMed Abstract: Clostridium perfringens is one of the most widely distributed and successful pathogens producing an impressive arsenal of toxins. One of the most potent toxins produced is the C. perfringens β-toxin (CPB). This toxin is the main virulence factor of type C strains. We describe the cryo-electron microscopy (EM) structure of CPB oligomer. We show that CPB forms homo-octameric pores like the hetero-oligomeric pores of the bi-component leukocidins, with important differences in the receptor binding region and the N-terminal latch domain. Intriguingly, the octameric CPB pore complex contains a second 16-stranded β-barrel protrusion atop of the cap domain that is formed by the N-termini of the eight protomers. We propose that CPB, together with the newly identified Epx toxins, is a member a new subclass of the hemolysin-like family. In addition, we show that the β-barrel protrusion domain can be modified without affecting the pore-forming ability, thus making the pore particularly attractive for macromolecule sensing and nanotechnology. The cryo-EM structure of the octameric pore of CPB will facilitate future developments in both nanotechnology and basic research. PubMed: 36215680DOI: 10.15252/embr.202254856 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.84 Å) |
Structure validation
Download full validation report