2j4y: Difference between revisions

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{{Seed}}
[[Image:2j4y.png|left|200px]]


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==Crystal structure of a rhodopsin stabilizing mutant expressed in mammalian cells==
The line below this paragraph, containing "STRUCTURE_2j4y", creates the "Structure Box" on the page.
<StructureSection load='2j4y' size='340' side='right'caption='[[2j4y]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2j4y]] 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=2J4Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J4Y FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</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>
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<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>
{{STRUCTURE_2j4y|  PDB=2j4y  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2j4y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j4y OCA], [https://pdbe.org/2j4y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j4y RCSB], [https://www.ebi.ac.uk/pdbsum/2j4y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j4y ProSAT]</span></td></tr>
</table>
== Function ==
[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/j4/2j4y_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2j4y ConSurf].
<div style="clear:both"></div>
<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.


===CRYSTAL STRUCTURE OF A RHODOPSIN STABILIZING MUTANT EXPRESSED IN MAMMALIAN CELLS===
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>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2j4y" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_17825322}}, adds the Publication Abstract to the page
*[[Rhodopsin 3D structures|Rhodopsin 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 17825322 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_17825322}}
__TOC__
 
</StructureSection>
==About this Structure==
2J4Y is a 2 chains structure of sequences 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=2J4Y OCA].
 
==Reference==
<ref group="xtra">PMID:17825322</ref><references group="xtra"/>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Burghammer, M.]]
[[Category: Large Structures]]
[[Category: Edwards, P C.]]
[[Category: Burghammer M]]
[[Category: Oprian, D D.]]
[[Category: Edwards PC]]
[[Category: Schertler, G F.X.]]
[[Category: Oprian DD]]
[[Category: Standfuss, J.]]
[[Category: Schertler GFX]]
[[Category: Xie, G.]]
[[Category: Standfuss J]]
[[Category: Acetylation]]
[[Category: Xie G]]
[[Category: Chromophore]]
[[Category: G-protein coupled receptor]]
[[Category: Glycoprotein]]
[[Category: Integral membrane protein]]
[[Category: Lipoprotein]]
[[Category: Membrane]]
[[Category: Palmitate]]
[[Category: Phosphorylation]]
[[Category: Photoreceptor]]
[[Category: Photoreceptor protein]]
[[Category: Receptor]]
[[Category: Retinal protein]]
[[Category: Sensory transduction]]
[[Category: Signaling protein]]
[[Category: Transducer]]
[[Category: Transmembrane]]
[[Category: Vision]]
[[Category: Visual pigment]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 22 10:35:44 2009''

Latest revision as of 10:56, 23 October 2024

Crystal structure of a rhodopsin stabilizing mutant expressed in mammalian cellsCrystal structure of a rhodopsin stabilizing mutant expressed in mammalian cells

Structural highlights

2j4y is a 2 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.4Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

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.

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 Also

References

  1. ↑ 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
  2. ↑ 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
  3. ↑ Standfuss J, Xie G, Edwards PC, Burghammer M, Oprian DD, Schertler GF. Crystal structure of a thermally stable rhodopsin mutant. J Mol Biol. 2007 Oct 5;372(5):1179-88. Epub 2007 Mar 12. PMID:17825322 doi:10.1016/j.jmb.2007.03.007

2j4y, resolution 3.40Å

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