1pfo
From Proteopedia
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| - | [[Image:1pfo.gif|left|200px]] | + | [[Image:1pfo.gif|left|200px]] |
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| - | '''PERFRINGOLYSIN O''' | + | {{Structure |
| + | |PDB= 1pfo |SIZE=350|CAPTION= <scene name='initialview01'>1pfo</scene>, resolution 2.2Å | ||
| + | |SITE= <scene name='pdbsite=ACT:Active+Site+CYS+Of+TRP-Rich+Motif'>ACT</scene> | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''PERFRINGOLYSIN O''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1PFO is a [ | + | 1PFO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_perfringens Clostridium perfringens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PFO OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9182756 9182756] |
[[Category: Clostridium perfringens]] | [[Category: Clostridium perfringens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: toxin]] | [[Category: toxin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:23:42 2008'' |
Revision as of 11:23, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Thu Mar 20 13:23:42 2008
