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TitleStructure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form.
Journal, issue, pagesCell, Vol. 89, Issue 5, Page 685-692, Year 1997
Publish dateMay 30, 1997
AuthorsJ Rossjohn / S C Feil / W J McKinstry / R K Tweten / M W Parker /
PubMed AbstractThe mechanisms by which proteins gain entry into membranes is a fundamental problem in biology. Here, we present the first crystal structure of a thiol-activated cytolysin, perfringolysin O, a member ...The mechanisms by which proteins gain entry into membranes is a fundamental problem in biology. Here, we present the first crystal structure of a thiol-activated cytolysin, perfringolysin O, a member of a large family of toxins that kill eukaryotic cells by punching holes in their membranes. The molecule adopts an unusually elongated shape rich in beta sheet. We have used electron microscopy data to construct a detailed model of the membrane channel form of the toxin. The structures reveal a novel mechanism for membrane insertion. Surprisingly, the toxin receptor, cholesterol, appears to play multiple roles: targeting, promotion of oligomerization, triggering a membrane insertion competent form, and stabilizing the membrane pore.
External linksCell / PubMed:9182756
MethodsX-ray diffraction
Resolution2.2 Å
Structure data

PDB-1pfo:
PERFRINGOLYSIN O
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

Chemicals

ChemComp-HOH:
WATER / Water

Source
  • clostridium perfringens (bacteria)
KeywordsTOXIN / THIOL-ACTIVATED CYTOLYSIN / HEMOLYSIS / CYTOLYSIS

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