3khe

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==Crystal structure of the calcium-loaded calmodulin-like domain of the CDPK, 541.m00134 from toxoplasma gondii==
==Crystal structure of the calcium-loaded calmodulin-like domain of the CDPK, 541.m00134 from toxoplasma gondii==
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<StructureSection load='3khe' size='340' side='right' caption='[[3khe]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
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<StructureSection load='3khe' size='340' side='right'caption='[[3khe]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3khe]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Toxoplasma_gondii Toxoplasma gondii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KHE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3KHE FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3khe]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Toxoplasma_gondii Toxoplasma gondii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KHE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KHE FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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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]] 1.95&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TGME49_105860 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5811 Toxoplasma gondii])</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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3khe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3khe OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3khe RCSB], [http://www.ebi.ac.uk/pdbsum/3khe PDBsum]</span></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=3khe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3khe OCA], [https://pdbe.org/3khe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3khe RCSB], [https://www.ebi.ac.uk/pdbsum/3khe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3khe ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q3HNM6_TOXGO Q3HNM6_TOXGO]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kh/3khe_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kh/3khe_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</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/chain_selection.php?pdb_ID=2ata ConSurf].
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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=3khe ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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We recently determined the first structures of inactivated and calcium-activated calcium-dependent protein kinases (CDPKs) from Apicomplexa. Calcium binding triggered a large conformational change that constituted a new mechanism in calcium signaling and a novel EF-hand fold (CAD, for CDPK activation domain). Thus we set out to determine if this mechanism was universal to all CDPKs. We solved additional CDPK structures, including one from the species Plasmodium. We highlight the similarities in sequence and structure across apicomplexan and plant CDPKs, and strengthen our observations that this novel mechanism could be universal to canonical CDPKs. Our new structures demonstrate more detailed steps in the mechanism of calcium activation and possible key players in regulation. Residues involved in making the largest conformational change are the most conserved across Apicomplexa, leading us to propose that the mechanism is indeed conserved. CpCDPK3_CAD and PfCDPK_CAD were captured at a possible intermediate conformation, lending insight into the order of activation steps. PfCDPK3_CAD adopts an activated fold, despite having an inactive EF-hand sequence in the N-terminal lobe. We propose that for most apicomplexan CDPKs, the mode of activation will be similar to that seen in our structures, while specific regulation of the inactive and active forms will require further investigation. Proteins 2011. (c) 2010 Wiley-Liss, Inc.
 
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Structures of parasitic CDPK domains point to a common mechanism of activation.,Wernimont AK, Amani M, Qiu W, Pizarro JC, Artz JD, Lin YH, Lew J, Hutchinson A, Hui R Proteins. 2011 Mar;79(3):803-20. doi: 10.1002/prot.22919. Epub 2010 Dec 3. PMID:21287613<ref>PMID:21287613</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
==See Also==
==See Also==
*[[Calcium-dependent protein kinase|Calcium-dependent protein kinase]]
*[[Calcium-dependent protein kinase|Calcium-dependent protein kinase]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Large Structures]]
[[Category: Toxoplasma gondii]]
[[Category: Toxoplasma gondii]]
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[[Category: Amani, M]]
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[[Category: Amani M]]
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[[Category: Arrowsmith, C H]]
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[[Category: Arrowsmith CH]]
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[[Category: Artz, J D]]
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[[Category: Artz JD]]
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[[Category: Bochkarev, A]]
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[[Category: Bochkarev A]]
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[[Category: Bountra, C]]
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[[Category: Bountra C]]
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[[Category: Cossar, D]]
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[[Category: Cossar D]]
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[[Category: Edwards, A M]]
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[[Category: Edwards AM]]
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[[Category: Hui, R]]
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[[Category: Hui R]]
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[[Category: Hutchinson, A]]
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[[Category: Hutchinson A]]
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[[Category: Kozieradzki, I]]
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[[Category: Kozieradzki I]]
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[[Category: Mackenzie, F]]
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[[Category: Mackenzie F]]
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[[Category: Qiu, W]]
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[[Category: Qiu W]]
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[[Category: Structural genomic]]
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[[Category: Weigelt J]]
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[[Category: Weigelt, J]]
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[[Category: Wernimont AK]]
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[[Category: Wernimont, A K]]
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[[Category: Atp-binding]]
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[[Category: Calcium dependent kinase]]
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[[Category: Kinase]]
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[[Category: Metal binding protein]]
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[[Category: Nucleotide-binding]]
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[[Category: Serine/threonine-protein kinase]]
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[[Category: Sgc]]
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Current revision

Crystal structure of the calcium-loaded calmodulin-like domain of the CDPK, 541.m00134 from toxoplasma gondii

PDB ID 3khe

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