1pfo
From Proteopedia
(Difference between revisions)
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<StructureSection load='1pfo' size='340' side='right'caption='[[1pfo]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='1pfo' size='340' side='right'caption='[[1pfo]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1pfo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1pfo]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PFO FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1pfo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pfo OCA], [https://pdbe.org/1pfo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pfo RCSB], [https://www.ebi.ac.uk/pdbsum/1pfo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pfo ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> |
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1pfo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pfo OCA], [https://pdbe.org/1pfo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pfo RCSB], [https://www.ebi.ac.uk/pdbsum/1pfo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pfo ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/TACY_CLOPE TACY_CLOPE] Sulfhydryl-activated toxin that causes cytolysis by forming pores in cholesterol containing host membranes. After binding to target membranes, the protein assembles into a pre-pore complex. A conformation change leads to insertion in the host membrane and formation of an oligomeric pore complex. Cholesterol may be required for binding to host cell membranes, membrane insertion and pore formation. Can be reversibly inactivated by oxidation.<ref>PMID:17328912</ref> | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1pfo ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1pfo ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | 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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| - | 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<ref>PMID:9182756</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1pfo" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Clostridium perfringens]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Parker | + | [[Category: Parker MW]] |
| - | [[Category: Rossjohn | + | [[Category: Rossjohn J]] |
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Current revision
PERFRINGOLYSIN O
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