1xji
From Proteopedia
(Difference between revisions)
(New page: 200px<br /><applet load="1xji" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xji, resolution 2.20Å" /> '''Bacteriorhodopsin cr...) |
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| - | [[Image:1xji.gif|left|200px]]<br /><applet load="1xji" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1xji, resolution 2.20Å" /> | ||
| - | '''Bacteriorhodopsin crystallized in bicelles at room temperature'''<br /> | ||
| - | == | + | ==Bacteriorhodopsin crystallized in bicelles at room temperature== |
| - | We showed previously that high-quality crystals of bacteriorhodopsin (bR) | + | <StructureSection load='1xji' size='340' side='right'caption='[[1xji]], [[Resolution|resolution]] 2.20Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1xji]] 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=1XJI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XJI FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C14:TETRADECANE'>C14</scene>, <scene name='pdbligand=CPS:3-[(3-CHOLAMIDOPROPYL)DIMETHYLAMMONIO]-1-PROPANESULFONATE'>CPS</scene>, <scene name='pdbligand=D10:DECANE'>D10</scene>, <scene name='pdbligand=D12:DODECANE'>D12</scene>, <scene name='pdbligand=OCT:N-OCTANE'>OCT</scene>, <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=1xji FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xji OCA], [https://pdbe.org/1xji PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xji RCSB], [https://www.ebi.ac.uk/pdbsum/1xji PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xji 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/xj/1xji_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1xji ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | We showed previously that high-quality crystals of bacteriorhodopsin (bR) from Halobacterium salinarum can be obtained from bicelle-forming DMPC/CHAPSO mixtures at 37 degrees C. As many membrane proteins are not sufficiently stable for crystallization at this high temperature, we tested whether the bicelle method could be applied at a lower temperature. Here we show that bR can be crystallized at room temperature using two different bicelle-forming compositions: DMPC/CHAPSO and DTPC/CHAPSO. The DTPC/CHAPSO crystals grown at room temperature are essentially identical to the previous, twinned crystals: space group P21 with unit cell dimensions of a = 44.7 A, b = 108.7 A, c = 55.8 A, beta = 113.6 degrees . The room-temperature DMPC/CHAPSO crystals are untwinned, however, and belong to space group C222(1) with the following unit cell dimensions: a = 44.7 A, b = 102.5 A, c = 128.2 A. The bR protein packs into almost identical layers in the two crystal forms, but the layers stack differently. The new untwinned crystal form yielded clear density for a previously unresolved CHAPSO molecule inserted between protein subunits within the layers. The ability to grow crystals at room temperature significantly expands the applicability of bicelle crystallization. | ||
| - | + | Crystallization of bacteriorhodopsin from bicelle formulations at room temperature.,Faham S, Boulting GL, Massey EA, Yohannan S, Yang D, Bowie JU Protein Sci. 2005 Mar;14(3):836-40. Epub 2005 Feb 2. PMID:15689517<ref>PMID:15689517</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1xji" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Bacteriorhodopsin 3D structures|Bacteriorhodopsin 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Halobacterium salinarum]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Boulting GL]] | ||
| + | [[Category: Bowie JU]] | ||
| + | [[Category: Faham S]] | ||
| + | [[Category: Massey EA]] | ||
| + | [[Category: Yang D]] | ||
| + | [[Category: Yohannan S]] | ||
Current revision
Bacteriorhodopsin crystallized in bicelles at room temperature
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