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3has
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of bacteriorhodopsin mutant L152A crystallized from bicelles== | |
| + | <StructureSection load='3has' size='340' side='right'caption='[[3has]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3has]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_halobius_ruber"_klebahn_1919 "bacillus halobius ruber" klebahn 1919]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HAS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HAS FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=HP6:HEPTANE'>HP6</scene>, <scene name='pdbligand=OCT:N-OCTANE'>OCT</scene>, <scene name='pdbligand=R16:HEXADECANE'>R16</scene>, <scene name='pdbligand=RET:RETINAL'>RET</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3hao|3hao]], [[3hap|3hap]], [[3haq|3haq]], [[3har|3har]]</div></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bop, VNG_1467G ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2242 "Bacillus halobius ruber" Klebahn 1919])</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=3has FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3has OCA], [https://pdbe.org/3has PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3has RCSB], [https://www.ebi.ac.uk/pdbsum/3has PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3has 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/ha/3has_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=3has ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | A major driving force for water-soluble protein folding is the hydrophobic effect, but membrane proteins cannot make use of this stabilizing contribution in the apolar core of the bilayer. It has been proposed that membrane proteins compensate by packing more efficiently. We therefore investigated packing contributions experimentally by observing the energetic and structural consequences of cavity creating mutations in the core of a membrane protein. We observed little difference in the packing energetics of water and membrane soluble proteins. Our results imply that other mechanisms are employed to stabilize the structure of membrane proteins. | ||
| - | + | Similar energetic contributions of packing in the core of membrane and water-soluble proteins.,Joh NH, Oberai A, Yang D, Whitelegge JP, Bowie JU J Am Chem Soc. 2009 Aug 12;131(31):10846-7. PMID:19603754<ref>PMID:19603754</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 3has" style="background-color:#fffaf0;"></div> | ||
| - | + | ==See Also== | |
| + | *[[Bacteriorhodopsin 3D structures|Bacteriorhodopsin 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Bacillus halobius ruber klebahn 1919]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Bowie, J U]] | ||
| + | [[Category: Joh, N H]] | ||
| + | [[Category: Yang, D]] | ||
| + | [[Category: Bacteriorhodopsin]] | ||
| + | [[Category: Cell membrane]] | ||
| + | [[Category: Chromophore]] | ||
| + | [[Category: Evolutionary constraint]] | ||
| + | [[Category: Helical membrane protein]] | ||
| + | [[Category: Hydrogen ion transport]] | ||
| + | [[Category: Integral membrane protein]] | ||
| + | [[Category: Ion transport]] | ||
| + | [[Category: Membrane]] | ||
| + | [[Category: Membrane protein]] | ||
| + | [[Category: Packing force]] | ||
| + | [[Category: Photoreceptor protein]] | ||
| + | [[Category: Proton transport]] | ||
| + | [[Category: Pyrrolidone carboxylic acid]] | ||
| + | [[Category: Receptor]] | ||
| + | [[Category: Retinal protein]] | ||
| + | [[Category: Sensory transduction]] | ||
| + | [[Category: Transmembrane]] | ||
| + | [[Category: Transport]] | ||
| + | [[Category: Transport protein]] | ||
| + | [[Category: Van der waal]] | ||
Current revision
Crystal structure of bacteriorhodopsin mutant L152A crystallized from bicelles
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Categories: Bacillus halobius ruber klebahn 1919 | Large Structures | Bowie, J U | Joh, N H | Yang, D | Bacteriorhodopsin | Cell membrane | Chromophore | Evolutionary constraint | Helical membrane protein | Hydrogen ion transport | Integral membrane protein | Ion transport | Membrane | Membrane protein | Packing force | Photoreceptor protein | Proton transport | Pyrrolidone carboxylic acid | Receptor | Retinal protein | Sensory transduction | Transmembrane | Transport | Transport protein | Van der waal
