This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1pfo
From Proteopedia
|
PERFRINGOLYSIN O
Overview
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.
About this Structure
1PFO is a Single protein structure of sequence from Clostridium perfringens. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 14:28:15 2008
