3c9m: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
 ==Structure of a mutant bovine rhodopsin in hexagonal crystal form==
-<StructureSection load='3c9m' size='340' side='right' caption='[[3c9m]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
+<StructureSection load='3c9m' size='340' side='right'caption='[[3c9m]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3c9m]] 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=3C9M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3C9M FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3c9m]] 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=3C9M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3C9M FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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]] 3.4&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2j4y|2j4y]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=3c9m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c9m OCA], [http://pdbe.org/3c9m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3c9m RCSB], [http://www.ebi.ac.uk/pdbsum/3c9m PDBsum]</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=3c9m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c9m OCA], [https://pdbe.org/3c9m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3c9m RCSB], [https://www.ebi.ac.uk/pdbsum/3c9m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3c9m 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>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
    <jmolCheckbox>
-     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c9/3c9m_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c9/3c9m_consurf.spt"</scriptWhenChecked>
      <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 21: / Line 22: @@
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
-We determined the structure of the rhodopsin mutant N2C/D282C expressed in mammalian cells; the first structure of a recombinantly produced G protein-coupled receptor (GPCR). The mutant was designed to form a disulfide bond between the N terminus and loop E3, which allows handling of opsin in detergent solution and increases thermal stability of rhodopsin by 10 deg.C. It allowed us to crystallize a fully deglycosylated rhodopsin (N2C/N15D/D282C). N15 mutations are normally misfolding and cause retinitis pigmentosa in humans. Microcrystallographic techniques and a 5 microm X-ray beam were used to collect data along a single needle measuring 5 microm x 5 microm x 90 microm. The disulfide introduces only minor changes but fixes the N-terminal cap over the beta-sheet lid covering the ligand-binding site, a likely explanation for the increased stability. This work allows structural investigation of rhodopsin mutants and shows the problems encountered during structure determination of GPCRs and other mammalian membrane proteins.
+The space-group symmetry of two crystal forms of rhodopsin (PDB codes 1gzm and 2j4y; space group P3(1)) can be re-interpreted as hexagonal (space group P6(4)). Two molecules of the G protein-coupled receptor are present in the asymmetric unit in the trigonal models. However, the noncrystallographic twofold axes parallel to the c axis can be treated as crystallographic symmetry operations in the hexagonal space group. This halves the asymmetric unit and makes all of the protein molecules equivalent in these structures. Corrections for merohedral twinning were also applied in the refinement in the higher symmetry space group for one of the structures (2j4y).
-Crystal structure of a thermally stable rhodopsin mutant.,Standfuss J, Xie G, Edwards PC, Burghammer M, Oprian DD, Schertler GF J Mol Biol. 2007 Oct 5;372(5):1179-88. Epub 2007 Mar 12. PMID:17825322<ref>PMID:17825322</ref>
+Alternative models for two crystal structures of bovine rhodopsin.,Stenkamp RE Acta Crystallogr D Biol Crystallogr. 2008 Aug;D64(Pt 8):902-4. Epub 2008, Jul 17. PMID:18645239<ref>PMID:18645239</ref>
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
@@ Line 30: / Line 31: @@
 ==See Also==
-*[[Rhodopsin|Rhodopsin]]
+*[[Rhodopsin 3D structures|Rhodopsin 3D structures]]
 == References ==
 <references/>
@@ Line 36: / Line 37: @@
 </StructureSection>
 [[Category: Bos taurus]]
-[[Category: Stenkamp, R E]]
+[[Category: Large Structures]]
-[[Category: Alternate space group]]
+[[Category: Stenkamp RE]]
-[[Category: Chromophore]]
-[[Category: G-protein coupled receptor]]
-[[Category: Glycoprotein]]
-[[Category: Integral membrane protein]]
-[[Category: Lipoprotein]]
-[[Category: Palmitate]]
-[[Category: Phosphoprotein]]
-[[Category: Phosphorylation]]
-[[Category: Photoreceptor]]
-[[Category: Photoreceptor protein]]
-[[Category: Receptor]]
-[[Category: Retinal protein]]
-[[Category: Sensory transduction]]
-[[Category: Signaling protein]]
-[[Category: Transducer]]
-[[Category: Transmembrane]]
-[[Category: Vision membrane]]
-[[Category: Visual pigment]]