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3pxo

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Crystal structure of Metarhodopsin II

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Retrieved from "http://52.214.119.220/wiki/index.php/3pxo"

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 ==Crystal structure of Metarhodopsin II==
-<StructureSection load='3pxo' size='340' side='right' caption='[[3pxo]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
+<StructureSection load='3pxo' size='340' side='right'caption='[[3pxo]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3pxo]] is a 1 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=3PXO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PXO FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3pxo]] is a 1 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=3PXO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PXO FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene>, <scene name='pdbligand=RET:RETINAL'>RET</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</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]] 3&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3pqr|3pqr]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3pxo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pxo OCA], [http://pdbe.org/3pxo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3pxo RCSB], [http://www.ebi.ac.uk/pdbsum/3pxo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3pxo ProSAT]</span></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=3pxo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pxo OCA], [https://pdbe.org/3pxo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pxo RCSB], [https://www.ebi.ac.uk/pdbsum/3pxo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pxo ProSAT]</span></td></tr>
 </table>
 == 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>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-G-protein-coupled receptors (GPCRs) are seven transmembrane helix (TM) proteins that transduce signals into living cells by binding extracellular ligands and coupling to intracellular heterotrimeric G proteins (Galphabetagamma). The photoreceptor rhodopsin couples to transducin and bears its ligand 11-cis-retinal covalently bound via a protonated Schiff base to the opsin apoprotein. Absorption of a photon causes retinal cis/trans isomerization and generates the agonist all-trans-retinal in situ. After early photoproducts, the active G-protein-binding intermediate metarhodopsin II (Meta II) is formed, in which the retinal Schiff base is still intact but deprotonated. Dissociation of the proton from the Schiff base breaks a major constraint in the protein and enables further activating steps, including an outward tilt of TM6 and formation of a large cytoplasmic crevice for uptake of the interacting C terminus of the Galpha subunit. Owing to Schiff base hydrolysis, Meta II is short-lived and notoriously difficult to crystallize. We therefore soaked opsin crystals with all-trans-retinal to form Meta II, presuming that the crystal's high concentration of opsin in an active conformation (Ops*) may facilitate all-trans-retinal uptake and Schiff base formation. Here we present the 3.0 A and 2.85 A crystal structures, respectively, of Meta II alone or in complex with an 11-amino-acid C-terminal fragment derived from Galpha (GalphaCT2). GalphaCT2 binds in a large crevice at the cytoplasmic side, akin to the binding of a similar Galpha-derived peptide to Ops* (ref. 7). In the Meta II structures, the electron density from the retinal ligand seamlessly continues into the Lys 296 side chain, reflecting proper formation of the Schiff base linkage. The retinal is in a relaxed conformation and almost undistorted compared with pure crystalline all-trans-retinal. By comparison with early photoproducts we propose how retinal translocation and rotation induce the gross conformational changes characteristic for Meta II. The structures can now serve as models for the large GPCR family.
-Crystal structure of metarhodopsin II.,Choe HW, Kim YJ, Park JH, Morizumi T, Pai EF, Krauss N, Hofmann KP, Scheerer P, Ernst OP Nature. 2011 Mar 9. PMID:21389988<ref>PMID:21389988</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3pxo" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Rhodopsin|Rhodopsin]]
+*[[Rhodopsin 3D structures|Rhodopsin 3D structures]]
 == References ==
 <references/>
@@ Line 27: / Line 18: @@
 </StructureSection>
 [[Category: Bos taurus]]
-[[Category: Choe, H W]]
+[[Category: Large Structures]]
-[[Category: Ernst, O P]]
+[[Category: Choe H-W]]
-[[Category: Hofmann, K P]]
+[[Category: Ernst OP]]
-[[Category: Kim, Y J]]
+[[Category: Hofmann KP]]
-[[Category: Krauss, N]]
+[[Category: Kim YJ]]
-[[Category: Morizumi, T]]
+[[Category: Krauss N]]
-[[Category: Pai, E F]]
+[[Category: Morizumi T]]
-[[Category: Park, J H]]
+[[Category: Pai EF]]
-[[Category: Scheerer, P]]
+[[Category: Park JH]]
-[[Category: Active state]]
+[[Category: Scheerer P]]
-[[Category: Chromophore]]
-[[Category: G-protein]]
-[[Category: G-protein coupled receptor]]
-[[Category: G-protein-coupled receptor]]
-[[Category: Galpha subunit]]
-[[Category: Glycoprotein]]
-[[Category: Gtp-binding]]
-[[Category: Lipoprotein]]
-[[Category: Membrane]]
-[[Category: Myristate]]
-[[Category: Nucleotide-binding]]
-[[Category: Opsin]]
-[[Category: Palmitate]]
-[[Category: Phosphoprotein]]
-[[Category: Photoreceptor]]
-[[Category: Photoreceptor protein]]
-[[Category: Protein]]
-[[Category: Receptor]]
-[[Category: Retinal protein]]
-[[Category: Rhodopsin]]
-[[Category: Sensory transduction]]
-[[Category: Signaling protein]]
-[[Category: Transducer]]
-[[Category: Transducin]]
-[[Category: Transmembrane]]
-[[Category: Vision]]

3pxo

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Crystal structure of Metarhodopsin II

Structural highlights

Function

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