1r2n: Difference between revisions

New page: left|200px<br /><applet load="1r2n" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r2n" /> '''NMR structure of the all-trans retinal in da...
 
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[[Image:1r2n.gif|left|200px]]<br /><applet load="1r2n" size="450" color="white" frame="true" align="right" spinBox="true"
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'''NMR structure of the all-trans retinal in dark-adapted Bacteriorhodopsin'''<br />


==Overview==
==NMR structure of the all-trans retinal in dark-adapted Bacteriorhodopsin==
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.
<StructureSection load='1r2n' size='340' side='right'caption='[[1r2n]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1r2n]] 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=1R2N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R2N FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1r2n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r2n OCA], [https://pdbe.org/1r2n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r2n RCSB], [https://www.ebi.ac.uk/pdbsum/1r2n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r2n ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BACR_HALSA BACR_HALSA] Light-driven proton pump.
== 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/r2/1r2n_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1r2n ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1R2N 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=1R2N OCA].
*[[Bacteriorhodopsin 3D structures|Bacteriorhodopsin 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
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]
[[Category: Halobacterium salinarum]]
[[Category: Halobacterium salinarum]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Kessler, B.]]
[[Category: Kessler B]]
[[Category: Kuhne, R.]]
[[Category: Kuhne R]]
[[Category: Oesterhaelt, D.]]
[[Category: Oesterhaelt D]]
[[Category: Oschkinat, H.]]
[[Category: Oschkinat H]]
[[Category: Patzelt, H.]]
[[Category: Patzelt H]]
[[Category: Schmieder, P.]]
[[Category: Schmieder P]]
[[Category: Simon, B.]]
[[Category: Simon B]]
[[Category: terLaak, A.]]
[[Category: TerLaak A]]
[[Category: RET]]
[[Category: haloarchaea]]
[[Category: membrane protein]]
[[Category: nmr]]
[[Category: photoreceptor]]
[[Category: proton pump]]
[[Category: proton transport]]
[[Category: retinal protein]]
 
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