2j4y: Difference between revisions
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<StructureSection load='2j4y' size='340' side='right' caption='[[2j4y]], [[Resolution|resolution]] 3.40Å' scene=''> | <StructureSection load='2j4y' size='340' side='right' caption='[[2j4y]], [[Resolution|resolution]] 3.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2j4y]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2j4y]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J4Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2J4Y FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=RET:RETINAL'>RET</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=RET:RETINAL'>RET</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1eds|1eds]], [[1edv|1edv]], [[1edw|1edw]], [[1edx|1edx]], [[1f88|1f88]], [[1fdf|1fdf]], [[1gzm|1gzm]], [[1hzx|1hzx]], [[1jfp|1jfp]], [[1l9h|1l9h]], [[1ln6|1ln6]], [[1n3m|1n3m]], [[1nzs|1nzs]], [[1ov0|1ov0]], [[1ov1|1ov1]], [[1u19|1u19]], [[1vqx|1vqx]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1eds|1eds]], [[1edv|1edv]], [[1edw|1edw]], [[1edx|1edx]], [[1f88|1f88]], [[1fdf|1fdf]], [[1gzm|1gzm]], [[1hzx|1hzx]], [[1jfp|1jfp]], [[1l9h|1l9h]], [[1ln6|1ln6]], [[1n3m|1n3m]], [[1nzs|1nzs]], [[1ov0|1ov0]], [[1ov1|1ov1]], [[1u19|1u19]], [[1vqx|1vqx]]</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=2j4y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j4y OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2j4y RCSB], [http://www.ebi.ac.uk/pdbsum/2j4y PDBsum]</span></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=2j4y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j4y OCA], [http://pdbe.org/2j4y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2j4y RCSB], [http://www.ebi.ac.uk/pdbsum/2j4y PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 2j4y" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Bovin]] | ||
[[Category: Burghammer, M]] | [[Category: Burghammer, M]] | ||
[[Category: Edwards, P C]] | [[Category: Edwards, P C]] | ||
Revision as of 18:45, 11 September 2015
Crystal structure of a rhodopsin stabilizing mutant expressed in mammalian cellsCrystal structure of a rhodopsin stabilizing mutant expressed in mammalian cells
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 PubMedWe 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. 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[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Bovin
- Burghammer, M
- Edwards, P C
- Oprian, D D
- Schertler, G F.X
- Standfuss, J
- Xie, G
- Chromophore
- G-protein coupled receptor
- Glycoprotein
- Integral membrane protein
- Lipoprotein
- Membrane
- Palmitate
- Phosphorylation
- Photoreceptor
- Photoreceptor protein
- Receptor
- Retinal protein
- Sensory transduction
- Signaling protein
- Transducer
- Transmembrane
- Vision
- Visual pigment