1pfo

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[[Image:1pfo.gif|left|200px]]
[[Image:1pfo.gif|left|200px]]
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{{Structure
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|SITE= <scene name='pdbsite=ACT:Active+Site+CYS+Of+TRP-Rich+Motif'>ACT</scene>
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{{STRUCTURE_1pfo| PDB=1pfo | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pfo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pfo OCA], [http://www.ebi.ac.uk/pdbsum/1pfo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pfo RCSB]</span>
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'''PERFRINGOLYSIN O'''
'''PERFRINGOLYSIN O'''
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[[Category: Parker, M W.]]
[[Category: Parker, M W.]]
[[Category: Rossjohn, J.]]
[[Category: Rossjohn, J.]]
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[[Category: cytolysis]]
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[[Category: Cytolysis]]
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[[Category: hemolysis]]
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[[Category: Hemolysis]]
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[[Category: thiol-activated cytolysin]]
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[[Category: Thiol-activated cytolysin]]
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[[Category: toxin]]
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[[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 Sun Mar 30 22:59:03 2008''
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Revision as of 02:01, 3 May 2008

Template:STRUCTURE 1pfo

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. 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 Sat May 3 05:01:55 2008

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