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1r84

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(New page: 200px<br /><applet load="1r84" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r84" /> '''NMR structure of the 13-cis-15-syn retinal i...)
Current revision (06:10, 17 April 2024) (edit) (undo)
 
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[[Image:1r84.jpg|left|200px]]<br /><applet load="1r84" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1r84" />
 
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'''NMR structure of the 13-cis-15-syn retinal in dark_adapted bacteriorhodopsin'''<br />
 
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==Overview==
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==NMR structure of the 13-cis-15-syn retinal in dark_adapted bacteriorhodopsin==
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The two forms of bacteriorhodopsin present in the dark-adapted state, containing either all-trans or 13-cis,15-syn retinal, were examined by, using solution state NMR, and their structures were determined. Comparison, of the all-trans and the 13-cis,15-syn forms shows a shift in position of, about 0.25 A within the pocket of the protein. Comparing this to the, 13-cis,15-anti chromophore of the catalytic cycle M-intermediate, structure, the 13-cis,15-syn form demonstrates a less pronounced up-tilt, of the retinal C12[bond]C14 region, while leaving W182 and T178, essentially unchanged. The N[bond]H dipole of the Schiff base orients, toward the extracellular side in both forms, however, it reorients toward, the intracellular side in the 13-cis,15-anti configuration to form the, catalytic M-intermediate. Thus, the change of the N[bond]H dipole is, considered primarily responsible for energy storage, conformation changes, of the protein, and the deprotonation of the Schiff base. The structural, similarity of the all-trans and 13-cis,15-syn forms is taken as strong, evidence for the ion dipole dragging model by which proton (hydroxide ion), translocation follows the change of the dipole.
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<StructureSection load='1r84' size='340' side='right'caption='[[1r84]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1r84]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Halobacterium_salinarum Halobacterium salinarum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R84 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R84 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=RET:RETINAL'>RET</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1r84 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r84 OCA], [https://pdbe.org/1r84 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r84 RCSB], [https://www.ebi.ac.uk/pdbsum/1r84 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r84 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/BACR_HALSA BACR_HALSA] Light-driven proton pump.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/r8/1r84_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1r84 ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1R84 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Halobacterium_salinarum Halobacterium salinarum] with RET as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1R84 OCA].
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*[[Bacteriorhodopsin 3D structures|Bacteriorhodopsin 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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The structures of the active center in dark-adapted bacteriorhodopsin by solution-state NMR spectroscopy., Patzelt H, Simon B, terLaak A, Kessler B, Kuhne R, Schmieder P, Oesterhelt D, Oschkinat H, Proc Natl Acad Sci U S A. 2002 Jul 23;99(15):9765-70. Epub 2002 Jul 15. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12119389 12119389]
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[[Category: Halobacterium salinarum]]
[[Category: Halobacterium salinarum]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Kessler, B.]]
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[[Category: Kessler B]]
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[[Category: Kuhne, R.]]
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[[Category: Kuhne R]]
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[[Category: Laak, A.Ter.]]
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[[Category: Oesterhaelt D]]
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[[Category: Oesterhaelt, D.]]
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[[Category: Oschkinat H]]
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[[Category: Oschkinat, H.]]
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[[Category: Patzelt H]]
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[[Category: Patzelt, H.]]
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[[Category: Schmieder P]]
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[[Category: Schmieder, P.]]
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[[Category: Simon B]]
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[[Category: Simon, B.]]
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[[Category: Ter Laak A]]
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[[Category: RET]]
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[[Category: haloarchea]]
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[[Category: membrane protein]]
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[[Category: nmr]]
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[[Category: photoreceptor]]
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[[Category: proton pump]]
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[[Category: proton transport]]
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[[Category: retinal protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:20:17 2007''
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Current revision

NMR structure of the 13-cis-15-syn retinal in dark_adapted bacteriorhodopsin

PDB ID 1r84

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