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3ku2
From Proteopedia
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| - | {{Seed}} | ||
| - | [[Image:3ku2.png|left|200px]] | ||
| - | < | + | ==Crystal Structure of inactivated form of CDPK1 from toxoplasma gondii, TGME49.101440== |
| - | + | <StructureSection load='3ku2' size='340' side='right'caption='[[3ku2]], [[Resolution|resolution]] 2.30Å' scene=''> | |
| - | You may | + | == Structural highlights == |
| - | + | <table><tr><td colspan='2'>[[3ku2]] is a 1 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=3KU2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KU2 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> | |
| - | - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></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=3ku2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ku2 OCA], [https://pdbe.org/3ku2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ku2 RCSB], [https://www.ebi.ac.uk/pdbsum/3ku2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ku2 ProSAT]</span></td></tr> | |
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q9BJF5_TOXGO Q9BJF5_TOXGO] | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ku/3ku2_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=3ku2 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Calcium-dependent protein kinases (CDPKs) have pivotal roles in the calcium-signaling pathway in plants, ciliates and apicomplexan parasites and comprise a calmodulin-dependent kinase (CaMK)-like kinase domain regulated by a calcium-binding domain in the C terminus. To understand this intramolecular mechanism of activation, we solved the structures of the autoinhibited (apo) and activated (calcium-bound) conformations of CDPKs from the apicomplexan parasites Toxoplasma gondii and Cryptosporidium parvum. In the apo form, the C-terminal CDPK activation domain (CAD) resembles a calmodulin protein with an unexpected long helix in the N terminus that inhibits the kinase domain in the same manner as CaMKII. Calcium binding triggers the reorganization of the CAD into a highly intricate fold, leading to its relocation around the base of the kinase domain to a site remote from the substrate binding site. This large conformational change constitutes a distinct mechanism in calcium signal-transduction pathways. | ||
| - | + | Structures of apicomplexan calcium-dependent protein kinases reveal mechanism of activation by calcium.,Wernimont AK, Artz JD, Finerty P Jr, Lin YH, Amani M, Allali-Hassani A, Senisterra G, Vedadi M, Tempel W, Mackenzie F, Chau I, Lourido S, Sibley LD, Hui R Nat Struct Mol Biol. 2010 May;17(5):596-601. Epub 2010 May 2. PMID:20436473<ref>PMID:20436473</ref> | |
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 3ku2" style="background-color:#fffaf0;"></div> | ||
| - | == | + | ==See Also== |
| - | + | *[[Calcium-dependent protein kinase|Calcium-dependent protein kinase]] | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Toxoplasma gondii]] | [[Category: Toxoplasma gondii]] | ||
| - | [[Category: Arrowsmith | + | [[Category: Arrowsmith CH]] |
| - | [[Category: Artz | + | [[Category: Artz JD]] |
| - | [[Category: Bochkarev | + | [[Category: Bochkarev A]] |
| - | [[Category: Bountra | + | [[Category: Bountra C]] |
| - | [[Category: Edwards | + | [[Category: Edwards AM]] |
| - | [[Category: Finnerty | + | [[Category: Finnerty P]] |
| - | [[Category: Hassani | + | [[Category: Hassani AA]] |
| - | [[Category: He | + | [[Category: He H]] |
| - | [[Category: Hui | + | [[Category: Hui R]] |
| - | [[Category: | + | [[Category: Lin YH]] |
| - | [[Category: | + | [[Category: Lourido S]] |
| - | [[Category: | + | [[Category: Mackenzie F]] |
| - | [[Category: Sibley | + | [[Category: Sibley DL]] |
| - | [[Category: Sinestera | + | [[Category: Sinestera G]] |
| - | [[Category: Vedadi | + | [[Category: Vedadi M]] |
| - | [[Category: Wasney | + | [[Category: Wasney G]] |
| - | [[Category: Weigelt | + | [[Category: Weigelt J]] |
| - | [[Category: Wernimont | + | [[Category: Wernimont AK]] |
| - | [[Category: Xiao | + | [[Category: Xiao T]] |
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Current revision
Crystal Structure of inactivated form of CDPK1 from toxoplasma gondii, TGME49.101440
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Categories: Large Structures | Toxoplasma gondii | Arrowsmith CH | Artz JD | Bochkarev A | Bountra C | Edwards AM | Finnerty P | Hassani AA | He H | Hui R | Lin YH | Lourido S | Mackenzie F | Sibley DL | Sinestera G | Vedadi M | Wasney G | Weigelt J | Wernimont AK | Xiao T


