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-Structure paper
タイトル | Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form. |
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ジャーナル・号・ページ | Cell, Vol. 89, Issue 5, Page 685-692, Year 1997 |
掲載日 | 1997年5月30日 |
![]() | J Rossjohn / S C Feil / W J McKinstry / R K Tweten / M W Parker / ![]() |
PubMed 要旨 | 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 ...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. |
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手法 | X線回折 |
解像度 | 2.2 Å |
構造データ | ![]() PDB-1pfo: |
化合物 | ![]() ChemComp-HOH: |
由来 |
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![]() | TOXIN / THIOL-ACTIVATED CYTOLYSIN / HEMOLYSIS / CYTOLYSIS |