7q9y
From Proteopedia
(Difference between revisions)
m (Protected "7q9y" [edit=sysop:move=sysop]) |
|||
| (2 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Cryo-EM structure of the octameric pore of Clostridium perfringens beta-toxin.== | |
| + | <StructureSection load='7q9y' size='340' side='right'caption='[[7q9y]], [[Resolution|resolution]] 3.84Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7q9y]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_perfringens_CPE Clostridium perfringens CPE]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7Q9Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Q9Y FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.84Å</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7q9y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7q9y OCA], [https://pdbe.org/7q9y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7q9y RCSB], [https://www.ebi.ac.uk/pdbsum/7q9y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7q9y ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q9L403_CLOPF Q9L403_CLOPF] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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 beta-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 beta-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 beta-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. | ||
| - | + | Cryo-EM structure of the octameric pore of Clostridium perfringens beta-toxin.,Bruggisser J, Iacovache I, Musson SC, Degiacomi MT, Posthaus H, Zuber B EMBO Rep. 2022 Dec 6;23(12):e54856. doi: 10.15252/embr.202254856. Epub 2022 Oct , 10. PMID:36215680<ref>PMID:36215680</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 7q9y" style="background-color:#fffaf0;"></div> |
| - | [[Category: Iacovache | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Clostridium perfringens CPE]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Iacovache I]] | ||
| + | [[Category: Zuber B]] | ||
Current revision
Cryo-EM structure of the octameric pore of Clostridium perfringens beta-toxin.
| |||||||||||
