1pfo

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[[Image:1pfo.gif|left|200px]]
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{{STRUCTURE_1pfo| PDB=1pfo | SCENE= }}
{{STRUCTURE_1pfo| PDB=1pfo | SCENE= }}
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'''PERFRINGOLYSIN O'''
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===PERFRINGOLYSIN O===
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==Overview==
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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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(as it appears on PubMed at http://www.pubmed.gov), where 9182756 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9182756}}
==About this Structure==
==About this Structure==
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[[Category: Thiol-activated cytolysin]]
[[Category: Thiol-activated cytolysin]]
[[Category: Toxin]]
[[Category: Toxin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:01:55 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 16:13:36 2008''

Revision as of 13:13, 28 July 2008

Image:1pfo.png

Template:STRUCTURE 1pfo

PERFRINGOLYSIN O

Template:ABSTRACT PUBMED 9182756

About this Structure

1PFO is a Single protein structure of sequence from Clostridium perfringens. 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 Mon Jul 28 16:13:36 2008

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