1r84: Difference between revisions
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<StructureSection load='1r84' size='340' side='right' caption='[[1r84]], [[NMR_Ensembles_of_Models | 12 NMR models]]' scene=''> | <StructureSection load='1r84' size='340' side='right' caption='[[1r84]], [[NMR_Ensembles_of_Models | 12 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1r84]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1r84]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_halobius_ruber"_klebahn_1919 "bacillus halobius ruber" klebahn 1919]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1R84 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=RET:RETINAL'>RET</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=RET:RETINAL'>RET</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1r2n|1r2n]], [[1brr|1brr]], [[1c3w|1c3w]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1r2n|1r2n]], [[1brr|1brr]], [[1c3w|1c3w]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1r84 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r84 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1r84 RCSB], [http://www.ebi.ac.uk/pdbsum/1r84 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1r84 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r84 OCA], [http://pdbe.org/1r84 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1r84 RCSB], [http://www.ebi.ac.uk/pdbsum/1r84 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1r84" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Bacillus halobius ruber klebahn 1919]] | ||
[[Category: Kessler, B]] | [[Category: Kessler, B]] | ||
[[Category: Kuhne, R]] | [[Category: Kuhne, R]] | ||
Revision as of 18:30, 10 September 2015
NMR structure of the 13-cis-15-syn retinal in dark_adapted bacteriorhodopsinNMR structure of the 13-cis-15-syn retinal in dark_adapted bacteriorhodopsin
Structural highlights
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. Publication Abstract from PubMedThe 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. 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:12119389[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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