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1iaz

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(New page: 200px<br /><applet load="1iaz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1iaz, resolution 1.9&Aring;" /> '''EQUINATOXIN II'''<br ...)
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[[Image:1iaz.gif|left|200px]]<br /><applet load="1iaz" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1iaz, resolution 1.9&Aring;" />
 
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'''EQUINATOXIN II'''<br />
 
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==Overview==
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==EQUINATOXIN II==
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BACKGROUND: Membrane pore-forming toxins have a remarkable property: they, adopt a stable soluble form structure, which, when in contact with a, membrane, undergoes a series of transformations, leading to an active, membrane-bound form. In contrast to bacterial toxins, no structure of a, pore-forming toxin from an eukaryotic organism has been determined so far, an indication that structural studies of equinatoxin II (EqtII) may, unravel a novel mechanism. RESULTS: The crystal structure of the soluble, form of EqtII from the sea anemone Actinia equina has been determined at, 1.9 A resolution. EqtII is shown to be a single-domain protein based on a, 12 strand beta sandwich fold with a hydrophobic core and a pair of alpha, helices, each of which is associated with the face of a beta sheet., CONCLUSIONS: The structure of the 30 N-terminal residues is the largest, segment that can adopt a different structure without disrupting the fold, of the beta sandwich core. This segment includes a three-turn alpha helix, that lies on the surface of a beta sheet and ends in a stretch of three, positively charged residues, Lys-30, Arg-31, and Lys-32. On the basis of, gathered data, it is suggested that this segment forms the membrane pore, whereas the beta sandwich structure remains unaltered and attaches to a, membrane as do other structurally related extrinsic membrane proteins or, their domains. The use of a structural data site-directed mutagenesis, study should reveal the residues involved in membrane pore formation.
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<StructureSection load='1iaz' size='340' side='right'caption='[[1iaz]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1iaz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Actinia_equina Actinia equina]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IAZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IAZ FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1iaz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iaz OCA], [https://pdbe.org/1iaz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iaz RCSB], [https://www.ebi.ac.uk/pdbsum/1iaz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iaz ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ACTP2_ACTEQ ACTP2_ACTEQ] Pore-forming protein that forms cations-selective hydrophilic pores of around 1 nm and causes cardiac stimulation and hemolysis. Pore formation is a multi-step process that involves specific recognition of membrane sphingomyelin (but neither cholesterol nor phosphatidylcholine) using aromatic rich region and adjacent phosphocholine (POC) binding site, firm binding to the membrane (mainly driven by hydrophobic interactions) accompanied by the transfer of the N-terminal region to the lipid-water interface and finally pore formation after oligomerization of several monomers. Cytolytic effects include red blood cells hemolysis, platelet aggregation and lysis, cytotoxic and cytostatic effects on fibroblasts. Lethality in mammals has been ascribed to severe vasospasm of coronary vessels, cardiac arrhythmia, and inotropic effects.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ia/1iaz_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1iaz ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1IAZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Actinia_equina Actinia equina] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IAZ OCA].
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*[[Cytolysin 3D structures|Cytolysin 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Crystal structure of the soluble form of equinatoxin II, a pore-forming toxin from the sea anemone Actinia equina., Athanasiadis A, Anderluh G, Macek P, Turk D, Structure. 2001 Apr 4;9(4):341-6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11525171 11525171]
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[[Category: Actinia equina]]
[[Category: Actinia equina]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Anderluh, G.]]
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[[Category: Anderluh G]]
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[[Category: Athanasiadis, A.]]
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[[Category: Athanasiadis A]]
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[[Category: Macek, P.]]
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[[Category: Macek P]]
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[[Category: Turk, D.]]
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[[Category: Turk D]]
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[[Category: SO4]]
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[[Category: beta-sandwich]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:13:47 2007''
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Current revision

EQUINATOXIN II

PDB ID 1iaz

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