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7Q9Y

Cryo-EM structure of the octameric pore of Clostridium perfringens beta-toxin.

Summary for 7Q9Y
Entry DOI10.2210/pdb7q9y/pdb
EMDB information13876
DescriptorClostridium perfringens beta toxin (1 entity in total)
Functional Keywordspore forming toxin, hemolysin, octamer, toxin
Biological sourceClostridium perfringens CPE
Total number of polymer chains8
Total formula weight279150.00
Authors
Iacovache, I.,Zuber, B. (deposition date: 2021-11-15, release date: 2022-10-19, Last modification date: 2024-07-17)
Primary citationBruggisser, 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: 36215680
DOI: 10.15252/embr.202254856
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.84 Å)
Structure validation

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