View source for 9epq


==Cryo-EM Structure of Jumping Spider Rhodopsin-1 bound to a Giq heterotrimer==
<StructureSection load='9epq' size='340' side='right'caption='[[9epq]], [[Resolution|resolution]] 4.15&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9epq]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Hasarius_adansoni Hasarius adansoni] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9EPQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9EPQ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.15&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A1H6M:(2~{E})-2-[3-[(1~{E},3~{E})-2-methyl-4-(2,6,6-trimethylcyclohexen-1-yl)buta-1,3-dienyl]cyclohex-2-en-1-ylidene]ethanal'>A1H6M</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=9epq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9epq OCA], [https://pdbe.org/9epq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9epq RCSB], [https://www.ebi.ac.uk/pdbsum/9epq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9epq ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/B1B1U5_9ARAC B1B1U5_9ARAC] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Opsins are G protein-coupled receptors (GPCRs) that have evolved to detect light stimuli and initiate intracellular signaling cascades. Their role as signal transducers is critical to light perception across the animal kingdom. Opsins covalently bind to the chromophore 11-cis retinal, which isomerizes to the all-trans isomer upon photon absorption, causing conformational changes that result in receptor activation. Monostable opsins, responsible for vision in vertebrates, release the chromophore after activation and must bind another retinal molecule to remain functional. In contrast, bistable opsins, responsible for non-visual light perception in vertebrates and for vision in invertebrates, absorb a second photon in the active state to return the chromophore and protein to the inactive state. Structures of bistable opsins in the activated state have proven elusive, limiting our understanding of how they function as bidirectional photoswitches. Here we present active state structures of a bistable opsin, jumping spider rhodopsin isoform-1 (JSR1), in complex with its downstream signaling partners, the G(i) and G(q) heterotrimers. These structures elucidate key differences in the activation mechanisms between monostable and bistable opsins, offering essential insights for the rational engineering of bistable opsins into diverse optogenetic tools to control G protein signaling pathways.

Active state structures of a bistable visual opsin bound to G proteins.,Tejero O, Pamula F, Koyanagi M, Nagata T, Afanasyev P, Das I, Deupi X, Sheves M, Terakita A, Schertler GFX, Rodrigues MJ, Tsai CJ Nat Commun. 2024 Oct 16;15(1):8928. doi: 10.1038/s41467-024-53208-2. PMID:39414813<ref>PMID:39414813</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9epq" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Hasarius adansoni]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Afanasyev P]]
[[Category: Das I]]
[[Category: Deupi X]]
[[Category: Koyanagi M]]
[[Category: Nagata T]]
[[Category: Pamula F]]
[[Category: Rodrigues MJ]]
[[Category: Schertler GFX]]
[[Category: Sheves M]]
[[Category: Tejero O]]
[[Category: Terakita A]]
[[Category: Tsai C-J]]