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3ekh

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Current revision (13:07, 30 August 2023) (edit) (undo)
 
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<StructureSection load='3ekh' size='340' side='right'caption='[[3ekh]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='3ekh' size='340' side='right'caption='[[3ekh]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3ekh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aeqvi Aeqvi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EKH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EKH FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3ekh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aequorea_victoria Aequorea victoria], [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EKH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EKH FirstGlance]. <br>
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</td></tr><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></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]] 2&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CRO:{2-[(1R,2R)-1-AMINO-2-HYDROXYPROPYL]-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>CRO</scene></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=CRO:{2-[(1R,2R)-1-AMINO-2-HYDROXYPROPYL]-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>CRO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3ek4|3ek4]], [[3ek7|3ek7]], [[3ek8|3ek8]], [[3ekj|3ekj]]</div></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Calm1, Calm, Cam, Cam1, CaMI ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6100 AEQVI])</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=3ekh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ekh OCA], [https://pdbe.org/3ekh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ekh RCSB], [https://www.ebi.ac.uk/pdbsum/3ekh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ekh ProSAT]</span></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=3ekh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ekh OCA], [https://pdbe.org/3ekh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ekh RCSB], [https://www.ebi.ac.uk/pdbsum/3ekh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ekh ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CALM1_RAT CALM1_RAT] Calmodulin mediates the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis. Mediates calcium-dependent inactivation of CACNA1C. Positively regulates calcium-activated potassium channel activity of KCNN2.[UniProtKB:P62158][https://www.uniprot.org/uniprot/MYLK_CHICK MYLK_CHICK] Phosphorylates a specific serine in the N-terminus of a myosin light chain, which leads to the formation of calmodulin/MLCK signal transduction complexes which allow selective transduction of calcium signals.[https://www.uniprot.org/uniprot/GFP_AEQVI GFP_AEQVI] Energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca(2+)-activated photoprotein aequorin.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Aeqvi]]
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[[Category: Aequorea victoria]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Akerboom, J]]
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[[Category: Rattus norvegicus]]
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[[Category: Looger, L L]]
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[[Category: Synthetic construct]]
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[[Category: Rivera, J D.Velez]]
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[[Category: Akerboom J]]
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[[Category: Schreiter, E R]]
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[[Category: Looger LL]]
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[[Category: Calmodulin]]
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[[Category: Schreiter ER]]
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[[Category: Cpegfp]]
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[[Category: Velez Rivera JD]]
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[[Category: Fluorescent protein]]
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[[Category: Gcamp2]]
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[[Category: Geci]]
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[[Category: M13 peptide]]
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[[Category: Signaling protein]]
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Current revision

Calcium-saturated GCaMP2 T116V/K378W mutant monomer

PDB ID 3ekh

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