1PFO

PERFRINGOLYSIN O

Summary for 1PFO

• Entry DOI: 10.2210/pdb1pfo/pdb
• Descriptor: PERFRINGOLYSIN O (2 entities in total)
• Functional Keywords: toxin, thiol-activated cytolysin, hemolysis, cytolysis
• Biological source: Clostridium perfringens
• Cellular location: Secreted: P19995
• Total number of polymer chains: 1
• Total formula weight: 55831.60

Authors

Rossjohn, J.,Parker, M.W. (deposition date: 1997-07-31, release date: 1998-08-05, Last modification date: 2024-02-14)

Primary citation

Rossjohn, J.,Feil, S.C.,McKinstry, W.J.,Tweten, R.K.,Parker, M.W.
Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form.
Cell(Cambridge,Mass.), 89:685-692, 1997

PubMed Abstract: 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.

PubMed: 9182756
DOI: 10.1016/S0092-8674(00)80251-2

Experimental method

X-RAY DIFFRACTION (2.2 Å)