9u9d
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Bipartite Genetically Encoded Biosensor sG-GECO1== | |
| + | <StructureSection load='9u9d' size='340' side='right'caption='[[9u9d]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[9u9d]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aequorea_victoria Aequorea victoria], [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus], [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=9U9D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9U9D 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]] 1.8Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9u9d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9u9d OCA], [https://pdbe.org/9u9d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9u9d RCSB], [https://www.ebi.ac.uk/pdbsum/9u9d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9u9d ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [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;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Self-complementing bipartite fluorescent proteins (FPs) are useful tools for the detection of protein-protein proximity and for localizing fluorophores to membrane-membrane contact sites. Here, we report versions of circularly permuted green FP (GFP), red FP (RFP), and mNeonGreen (NG), which are split into a large fragment composed of nine beta-strands and a small fragment composed of two beta-strands. In each case, the large and small fragments can associate in live cells to form the complete 11-stranded FP beta-barrel. We further converted each of these three self-complementing FPs into bipartite calcium ion (Ca(2+)) biosensors. We demonstrate that appropriately targeted versions of these split FPs, and split FP-based biosensors, can be functionally assembled at membrane-membrane contact sites. We employ the bipartite NG-based Ca(2+) biosensor for visualization of pharmacologically induced Ca(2+) release at mitochondria-endoplasmic reticulum contact sites (MERCs). | ||
| - | + | Bipartite Genetically Encoded Biosensors to Sense Calcium Ion Dynamics at Membrane-Membrane Contact Sites.,Yamaguchi I, Barazzuol L, Dematteis G, Zhu W, Wen Y, Drobizhev M, Lim D, Campbell RE, Cali T, Nasu Y Anal Chem. 2025 Sep 16;97(36):19848-19861. doi: 10.1021/acs.analchem.5c03831. , Epub 2025 Sep 1. PMID:40888292<ref>PMID:40888292</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 9u9d" style="background-color:#fffaf0;"></div> |
| - | [[Category: Campbell | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Aequorea victoria]] | ||
| + | [[Category: Gallus gallus]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Rattus norvegicus]] | ||
| + | [[Category: Synthetic construct]] | ||
| + | [[Category: Campbell RE]] | ||
| + | [[Category: Wen Y]] | ||
Current revision
Bipartite Genetically Encoded Biosensor sG-GECO1
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