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| | <StructureSection load='2ziy' size='340' side='right'caption='[[2ziy]], [[Resolution|resolution]] 3.70Å' scene=''> | | <StructureSection load='2ziy' size='340' side='right'caption='[[2ziy]], [[Resolution|resolution]] 3.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2ziy]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Todarodes_pacificus Todarodes pacificus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZIY OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2ZIY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2ziy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Todarodes_pacificus Todarodes pacificus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZIY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZIY FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene>, <scene name='pdbligand=RET:RETINAL'>RET</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]] 3.7Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2ziy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ziy OCA], [http://pdbe.org/2ziy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ziy RCSB], [http://www.ebi.ac.uk/pdbsum/2ziy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ziy ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene>, <scene name='pdbligand=RET:RETINAL'>RET</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=2ziy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ziy OCA], [https://pdbe.org/2ziy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ziy RCSB], [https://www.ebi.ac.uk/pdbsum/2ziy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ziy ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/OPSD_TODPA OPSD_TODPA]] Visual pigments such as rhodopsin and porphyropsin are light-absorbing molecules that mediate vision. Rhodopsin consists of an apoprotein, opsin, covalently linked to 11-cis-retinal. This receptor is coupled to the activation of phospholipase C. Porphyropsin consists of opsin covalently linked to 11-cis 3,4-didehydroretinal. | + | [https://www.uniprot.org/uniprot/OPSD_TODPA OPSD_TODPA] Visual pigments such as rhodopsin and porphyropsin are light-absorbing molecules that mediate vision. Rhodopsin consists of an apoprotein, opsin, covalently linked to 11-cis-retinal. This receptor is coupled to the activation of phospholipase C. Porphyropsin consists of opsin covalently linked to 11-cis 3,4-didehydroretinal. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Todarodes pacificus]] | | [[Category: Todarodes pacificus]] |
| - | [[Category: Miyano, M]] | + | [[Category: Miyano M]] |
| - | [[Category: Shimamura, T]] | + | [[Category: Shimamura T]] |
| - | [[Category: Chromophore]]
| + | |
| - | [[Category: G-protein coupled receptor]]
| + | |
| - | [[Category: Glycoprotein]]
| + | |
| - | [[Category: Lipoprotein]]
| + | |
| - | [[Category: Palmitate]]
| + | |
| - | [[Category: Phosphoprotein]]
| + | |
| - | [[Category: Photoreceptor protein]]
| + | |
| - | [[Category: Receptor]]
| + | |
| - | [[Category: Retinal protein]]
| + | |
| - | [[Category: Sensory transduction]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
| - | [[Category: Transducer]]
| + | |
| - | [[Category: Transmembrane helice]]
| + | |
| - | [[Category: Vision]]
| + | |
| Structural highlights
Function
OPSD_TODPA Visual pigments such as rhodopsin and porphyropsin are light-absorbing molecules that mediate vision. Rhodopsin consists of an apoprotein, opsin, covalently linked to 11-cis-retinal. This receptor is coupled to the activation of phospholipase C. Porphyropsin consists of opsin covalently linked to 11-cis 3,4-didehydroretinal.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
G-protein-coupled receptors play a key step in cellular signal transduction cascades by transducing various extracellular signals via G-proteins. Rhodopsin is a prototypical G-protein-coupled receptor involved in the retinal visual signaling cascade. We determined the structure of squid rhodopsin at 3.7A resolution, which transduces signals through the G(q) protein to the phosphoinositol cascade. The structure showed seven transmembrane helices and an amphipathic helix H8 has similar geometry to structures from bovine rhodopsin, coupling to G(t), and human beta(2)-adrenergic receptor, coupling to G(s). Notably, squid rhodopsin contains a well structured cytoplasmic region involved in the interaction with G-proteins, and this region is flexible or disordered in bovine rhodopsin and human beta(2)-adrenergic receptor. The transmembrane helices 5 and 6 are longer and extrude into the cytoplasm. The distal C-terminal tail contains a short hydrophilic alpha-helix CH after the palmitoylated cysteine residues. The residues in the distal C-terminal tail interact with the neighboring residues in the second cytoplasmic loop, the extruded transmembrane helices 5 and 6, and the short helix H8. Additionally, the Tyr-111, Asn-87, and Asn-185 residues are located within hydrogen-bonding distances from the nitrogen atom of the Schiff base.
Crystal structure of squid rhodopsin with intracellularly extended cytoplasmic region.,Shimamura T, Hiraki K, Takahashi N, Hori T, Ago H, Masuda K, Takio K, Ishiguro M, Miyano M J Biol Chem. 2008 Jun 27;283(26):17753-6. Epub 2008 May 6. PMID:18463093[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Shimamura T, Hiraki K, Takahashi N, Hori T, Ago H, Masuda K, Takio K, Ishiguro M, Miyano M. Crystal structure of squid rhodopsin with intracellularly extended cytoplasmic region. J Biol Chem. 2008 Jun 27;283(26):17753-6. Epub 2008 May 6. PMID:18463093 doi:10.1074/jbc.C800040200
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