7aug
From Proteopedia
(Difference between revisions)
| (One intermediate revision not shown.) | |||
| Line 1: | Line 1: | ||
==Crystal structure of rsGCamP1.3 in the ON state== | ==Crystal structure of rsGCamP1.3 in the ON state== | ||
| - | <StructureSection load='7aug' size='340' side='right'caption='[[7aug]]' scene=''> | + | <StructureSection load='7aug' size='340' side='right'caption='[[7aug]], [[Resolution|resolution]] 2.04Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7AUG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7AUG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7aug]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aequorea_victoria Aequorea victoria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7AUG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7AUG FirstGlance]. <br> |
| - | </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=7aug FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7aug OCA], [https://pdbe.org/7aug PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7aug RCSB], [https://www.ebi.ac.uk/pdbsum/7aug PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7aug ProSAT]</span></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]] 2.04Å</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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=PIA:[(4Z)-2-[(1S)-1-AMINOETHYL]-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL]ACETIC+ACID'>PIA</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=7aug FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7aug OCA], [https://pdbe.org/7aug PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7aug RCSB], [https://www.ebi.ac.uk/pdbsum/7aug PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7aug ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Disease == | ||
| + | [https://www.uniprot.org/uniprot/CALM1_HUMAN CALM1_HUMAN] The disease is caused by mutations affecting the gene represented in this entry. Mutations in CALM1 are the cause of CPVT4. The disease is caused by mutations affecting the gene represented in this entry. Mutations in CALM1 are the cause of LQT14. | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CALM1_HUMAN CALM1_HUMAN] 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 (PubMed:16760425). Mediates calcium-dependent inactivation of CACNA1C (PubMed:26969752). Positively regulates calcium-activated potassium channel activity of KCNN2 (PubMed:27165696).<ref>PMID:16760425</ref> <ref>PMID:23893133</ref> <ref>PMID:26969752</ref> <ref>PMID:27165696</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Reversibly photo-switchable proteins are essential for many super-resolution fluorescence microscopic and optoacoustic imaging methods. However, they have yet to be used as sensors that measure the distribution of specific analytes at the nanoscale or in the tissues of live animals. Here we constructed the prototype of a photo-switchable Ca(2+) sensor based on GCaMP5G that can be switched with 405/488-nm light and describe its molecular mechanisms at the structural level, including the importance of the interaction of the core barrel structure of the fluorescent protein with the Ca(2+) receptor moiety. We demonstrate super-resolution imaging of Ca(2+) concentration in cultured cells and optoacoustic Ca(2+) imaging in implanted tumor cells in mice under controlled Ca(2+) conditions. Finally, we show the generalizability of the concept by constructing examples of photo-switching maltose and dopamine sensors based on periplasmatic binding protein and G-protein-coupled receptor-based sensors. | ||
| + | |||
| + | Genetically encoded photo-switchable molecular sensors for optoacoustic and super-resolution imaging.,Mishra K, Fuenzalida-Werner JP, Pennacchietti F, Janowski R, Chmyrov A, Huang Y, Zakian C, Klemm U, Testa I, Niessing D, Ntziachristos V, Stiel AC Nat Biotechnol. 2021 Nov 29. pii: 10.1038/s41587-021-01100-5. doi:, 10.1038/s41587-021-01100-5. PMID:34845372<ref>PMID:34845372</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7aug" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Aequorea victoria]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Fuenzalida-Werner JP]] | [[Category: Fuenzalida-Werner JP]] | ||
Current revision
Crystal structure of rsGCamP1.3 in the ON state
| |||||||||||
