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| | <StructureSection load='3cap' size='340' side='right'caption='[[3cap]], [[Resolution|resolution]] 2.90Å' scene=''> | | <StructureSection load='3cap' size='340' side='right'caption='[[3cap]], [[Resolution|resolution]] 2.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3cap]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CAP OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3CAP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3cap]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CAP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CAP FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGL:B-2-OCTYLGLUCOSIDE'>BGL</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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]] 2.9Å</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=3cap FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cap OCA], [http://pdbe.org/3cap PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3cap RCSB], [http://www.ebi.ac.uk/pdbsum/3cap PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3cap ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGL:B-2-OCTYLGLUCOSIDE'>BGL</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</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=3cap FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cap OCA], [https://pdbe.org/3cap PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cap RCSB], [https://www.ebi.ac.uk/pdbsum/3cap PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cap ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/OPSD_BOVIN OPSD_BOVIN]] Photoreceptor required for image-forming vision at low light intensity. Required for photoreceptor cell viability after birth. Light-induced isomerization of 11-cis to all-trans retinal triggers a conformational change leading to G-protein activation and release of all-trans retinal (By similarity).<ref>PMID:16908857</ref> <ref>PMID:17060607</ref> | + | [https://www.uniprot.org/uniprot/OPSD_BOVIN OPSD_BOVIN] Photoreceptor required for image-forming vision at low light intensity. Required for photoreceptor cell viability after birth. Light-induced isomerization of 11-cis to all-trans retinal triggers a conformational change leading to G-protein activation and release of all-trans retinal (By similarity).<ref>PMID:16908857</ref> <ref>PMID:17060607</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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Line 39: |
| | [[Category: Bos taurus]] | | [[Category: Bos taurus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Choe, H W]] | + | [[Category: Choe H-W]] |
| - | [[Category: Ernst, O P]] | + | [[Category: Ernst OP]] |
| - | [[Category: Hofmann, K P]] | + | [[Category: Hofmann KP]] |
| - | [[Category: Park, J H]] | + | [[Category: Park JH]] |
| - | [[Category: Scheerer, P]] | + | [[Category: Scheerer P]] |
| - | [[Category: Chromophore]]
| + | |
| - | [[Category: G protein-coupled receptor]]
| + | |
| - | [[Category: G-protein coupled receptor]]
| + | |
| - | [[Category: Glycoprotein]]
| + | |
| - | [[Category: Ligand-free state]]
| + | |
| - | [[Category: Lipoprotein]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Opsin]]
| + | |
| - | [[Category: Palmitate]]
| + | |
| - | [[Category: Phosphoprotein]]
| + | |
| - | [[Category: Photoreceptor]]
| + | |
| - | [[Category: Photoreceptor protein]]
| + | |
| - | [[Category: Retinal protein]]
| + | |
| - | [[Category: Rhodopsin]]
| + | |
| - | [[Category: Sensory transduction]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
| - | [[Category: Transducer]]
| + | |
| - | [[Category: Transmembrane]]
| + | |
| - | [[Category: Vision]]
| + | |
| Structural highlights
Function
OPSD_BOVIN Photoreceptor required for image-forming vision at low light intensity. Required for photoreceptor cell viability after birth. Light-induced isomerization of 11-cis to all-trans retinal triggers a conformational change leading to G-protein activation and release of all-trans retinal (By similarity).[1] [2]
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
In the G-protein-coupled receptor (GPCR) rhodopsin, the inactivating ligand 11-cis-retinal is bound in the seven-transmembrane helix (TM) bundle and is cis/trans isomerized by light to form active metarhodopsin II. With metarhodopsin II decay, all-trans-retinal is released, and opsin is reloaded with new 11-cis-retinal. Here we present the crystal structure of ligand-free native opsin from bovine retinal rod cells at 2.9 angstrom (A) resolution. Compared to rhodopsin, opsin shows prominent structural changes in the conserved E(D)RY and NPxxY(x)(5,6)F regions and in TM5-TM7. At the cytoplasmic side, TM6 is tilted outwards by 6-7 A, whereas the helix structure of TM5 is more elongated and close to TM6. These structural changes, some of which were attributed to an active GPCR state, reorganize the empty retinal-binding pocket to disclose two openings that may serve the entry and exit of retinal. The opsin structure sheds new light on ligand binding to GPCRs and on GPCR activation.
Crystal structure of the ligand-free G-protein-coupled receptor opsin.,Park JH, Scheerer P, Hofmann KP, Choe HW, Ernst OP Nature. 2008 Jul 10;454(7201):183-7. Epub 2008 Jun 18. PMID:18563085[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Nakamichi H, Okada T. Local peptide movement in the photoreaction intermediate of rhodopsin. Proc Natl Acad Sci U S A. 2006 Aug 22;103(34):12729-34. Epub 2006 Aug 14. PMID:16908857
- ↑ Salom D, Lodowski DT, Stenkamp RE, Le Trong I, Golczak M, Jastrzebska B, Harris T, Ballesteros JA, Palczewski K. Crystal structure of a photoactivated deprotonated intermediate of rhodopsin. Proc Natl Acad Sci U S A. 2006 Oct 31;103(44):16123-8. Epub 2006 Oct 23. PMID:17060607
- ↑ Park JH, Scheerer P, Hofmann KP, Choe HW, Ernst OP. Crystal structure of the ligand-free G-protein-coupled receptor opsin. Nature. 2008 Jul 10;454(7201):183-7. Epub 2008 Jun 18. PMID:18563085 doi:10.1038/nature07063
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