1pfo
From Proteopedia
PERFRINGOLYSIN O
Structural highlights
Function[TACY_CLOPE] Sulfhydryl-activated toxin that causes cytolysis by forming pores in cholesterol containing host membranes. After binding to target membranes, the protein assembles into a pre-pore complex. A conformation change leads to insertion in the host membrane and formation of an oligomeric pore complex. Cholesterol may be required for binding to host cell membranes, membrane insertion and pore formation. Can be reversibly inactivated by oxidation.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form.,Rossjohn J, Feil SC, McKinstry WJ, Tweten RK, Parker MW Cell. 1997 May 30;89(5):685-92. PMID:9182756[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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