1r2n: Difference between revisions

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[[Image:1r2n.gif|left|200px]]


{{Structure
==NMR structure of the all-trans retinal in dark-adapted Bacteriorhodopsin==
|PDB= 1r2n |SIZE=350|CAPTION= <scene name='initialview01'>1r2n</scene>
<StructureSection load='1r2n' size='340' side='right'caption='[[1r2n]]' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=RET:RETINAL'>RET</scene>
<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>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
|GENE=  
<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>
|DOMAIN=
<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>
|RELATEDENTRY=[[1brr|1BRR]], [[1c3w|1c3w]], [[1qhj|1qhj]]
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1r2n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r2n OCA], [http://www.ebi.ac.uk/pdbsum/1r2n PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1r2n RCSB]</span>
== 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>


'''NMR structure of the all-trans retinal in dark-adapted Bacteriorhodopsin'''
==See Also==
 
*[[Bacteriorhodopsin 3D structures|Bacteriorhodopsin 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
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.
 
==About this Structure==
1R2N is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Halobacterium_salinarum Halobacterium salinarum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R2N OCA].
 
==Reference==
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://www.ncbi.nlm.nih.gov/pubmed/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: haloarchaea]]
[[Category: membrane protein]]
[[Category: nmr]]
[[Category: photoreceptor]]
[[Category: proton pump]]
[[Category: proton transport]]
[[Category: retinal protein]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:22:23 2008''

Latest revision as of 09:08, 17 April 2024

NMR structure of the all-trans retinal in dark-adapted BacteriorhodopsinNMR structure of the all-trans retinal in dark-adapted Bacteriorhodopsin

Structural highlights

1r2n is a 1 chain structure with sequence from Halobacterium salinarum. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

BACR_HALSA Light-driven proton pump.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

Drag the structure with the mouse to rotate

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