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==CRYSTAL STRUCTURE OF AEQUORIN==
==CRYSTAL STRUCTURE OF AEQUORIN==
<StructureSection load='1ej3' size='340' side='right' caption='[[1ej3]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='1ej3' size='340' side='right'caption='[[1ej3]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1ej3]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EJ3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EJ3 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1ej3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aequorea_forskalea Aequorea forskalea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EJ3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EJ3 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CZH:C2-HYDROPEROXY-COELENTERAZINE'>CZH</scene></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]] 2.3&#8491;</td></tr>
<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=1ej3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ej3 OCA], [http://pdbe.org/1ej3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ej3 RCSB], [http://www.ebi.ac.uk/pdbsum/1ej3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ej3 ProSAT]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CZH:C2-HYDROPEROXY-COELENTERAZINE'>CZH</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=1ej3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ej3 OCA], [https://pdbe.org/1ej3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ej3 RCSB], [https://www.ebi.ac.uk/pdbsum/1ej3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ej3 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/AEQ2_AEQVI AEQ2_AEQVI]] Ca(2+)-dependent bioluminescence photoprotein. Displays an emission peak at 470 nm (blue light). Trace amounts of calcium ion trigger the intramolecular oxidation of the chromophore, coelenterazine into coelenteramide and CO(2) with the concomitant emission of light.  
[https://www.uniprot.org/uniprot/AEQ2_AEQVI AEQ2_AEQVI] Ca(2+)-dependent bioluminescence photoprotein. Displays an emission peak at 470 nm (blue light). Trace amounts of calcium ion trigger the intramolecular oxidation of the chromophore, coelenterazine into coelenteramide and CO(2) with the concomitant emission of light.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ej/1ej3_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ej/1ej3_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>
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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=1ej3 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=1ej3 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Aequorin is a calcium-sensitive photoprotein originally obtained from the jellyfish Aequorea aequorea. Because it has a high sensitivity to calcium ions and is biologically harmless, aequorin is widely used as a probe to monitor intracellular levels of free calcium. The aequorin molecule contains four helix-loop-helix 'EF-hand' domains, of which three can bind calcium. The molecule also contains coelenterazine as its chromophoric ligand. When calcium is added, the protein complex decomposes into apoaequorin, coelenteramide and CO2, accompanied by the emission of light. Apoaequorin can be regenerated into active aequorin in the absence of calcium by incubation with coelenterazine, oxygen and a thiol agent. Cloning and expression of the complementary DNA for aequorin were first reported in 1985 (refs 2, 6), and growth of crystals of the recombinant protein has been described; however, techniques have only recently been developed to prepare recombinant aequorin of the highest purity, permitting a full crystallographic study. Here we report the structure of recombinant aequorin determined by X-ray crystallography. Aequorin is found to be a globular molecule containing a hydrophobic core cavity that accommodates the ligand coelenterazine-2-hydroperoxide. The structure shows protein components stabilizing the peroxide and suggests a mechanism by which calcium activation may occur.
The crystal structure of the photoprotein aequorin at 2.3 A resolution.,Head JF, Inouye S, Teranishi K, Shimomura O Nature. 2000 May 18;405(6784):372-6. PMID:10830969<ref>PMID:10830969</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1ej3" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Head, J F]]
[[Category: Aequorea forskalea]]
[[Category: Inouye, S]]
[[Category: Large Structures]]
[[Category: Shimomura, O]]
[[Category: Head JF]]
[[Category: Teranishi, K]]
[[Category: Inouye S]]
[[Category: Four ef-hand calcium-binding protein]]
[[Category: Shimomura O]]
[[Category: Oxidoreductase]]
[[Category: Teranishi K]]
[[Category: Protein-coelenterazine peroxide complex]]
Retrieved from "https://proteopedia.org/1ej3"