1e0p

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[[Image:1e0p.gif|left|200px]]<br />
 
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<applet load="1e0p" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1e0p, resolution 2.1&Aring;" />
 
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'''L INTERMEDIATE OF BACTERIORHODOPSIN'''<br />
 
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==Overview==
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==L intermediate of bacteriorhodopsin==
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A wide variety of mechanisms are used to generate a proton-motive, potential across cell membranes, a function lying at the heart of, bioenergetics. Bacteriorhodopsin, the simplest known proton pump, provides, a paradigm for understanding this process. Here we report, at 2.1 A, resolution, the structural changes in bacteriorhodopsin immediately, preceding the primary proton transfer event in its photocycle. The early, structural rearrangements propagate from the protein's core towards the, extracellular surface, disrupting the network of hydrogen-bonded water, molecules that stabilizes helix C in the ground state. Concomitantly, a, bend of this helix enables the negatively charged primary proton acceptor, Asp 85, to approach closer to the positively charged primary proton donor, the Schiff base. The primary proton transfer event would then neutralize, these two groups, cancelling their electrostatic attraction and, facilitating a relaxation of helix C to a less strained geometry., Reprotonation of the Schiff base by Asp 85 would thereby be impeded, ensuring vectorial proton transport. Structural rearrangements also occur, near the protein's surface, aiding proton release to the extracellular, medium.
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<StructureSection load='1e0p' size='340' side='right'caption='[[1e0p]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1e0p]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Halobacterium_salinarum Halobacterium salinarum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E0P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E0P 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">X-ray diffraction, [[Resolution|Resolution]] 2.1&#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=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=1e0p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e0p OCA], [https://pdbe.org/1e0p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e0p RCSB], [https://www.ebi.ac.uk/pdbsum/1e0p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e0p 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/e0/1e0p_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=1e0p 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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1E0P 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]. Structure known Active Sites: AC1 and AC2. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E0P 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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Helix deformation is coupled to vectorial proton transport in the photocycle of bacteriorhodopsin., Royant A, Edman K, Ursby T, Pebay-Peyroula E, Landau EM, Neutze R, Nature. 2000 Aug 10;406(6796):645-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10949307 10949307]
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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: Edman, K.]]
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[[Category: Edman K]]
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[[Category: Landau, E.M.]]
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[[Category: Landau EM]]
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[[Category: Neutze, R.]]
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[[Category: Neutze R]]
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[[Category: Pebay-Peyroula, E.]]
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[[Category: Pebay-Peyroula E]]
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[[Category: Royant, A.]]
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[[Category: Royant A]]
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[[Category: Ursby, T.]]
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[[Category: Ursby T]]
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[[Category: RET]]
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[[Category: ion transport]]
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[[Category: photoreceptor]]
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[[Category: retinal protein hydrogen ion transport]]
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[[Category: transmembrane]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 14:53:47 2007''
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Current revision

L intermediate of bacteriorhodopsin

PDB ID 1e0p

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