4xxj
From Proteopedia
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| - | ''' | + | ==Crystal Structure of Escherichia coli-Expressed Halobacterium salinarum Bacteriorhodopsin in the Trimeric Form== |
| + | <StructureSection load='4xxj' size='340' side='right' caption='[[4xxj]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4xxj]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XXJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XXJ FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LFA:EICOSANE'>LFA</scene>, <scene name='pdbligand=MPG:1-MONOOLEOYL-RAC-GLYCEROL'>MPG</scene></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LYR:N~6~-[(2Z,4E,6E,8E)-3,7-DIMETHYL-9-(2,6,6-TRIMETHYLCYCLOHEX-1-EN-1-YL)NONA-2,4,6,8-TETRAENYL]LYSINE'>LYR</scene></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=4xxj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xxj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4xxj RCSB], [http://www.ebi.ac.uk/pdbsum/4xxj PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/BACR_HALSA BACR_HALSA]] Light-driven proton pump. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Heterologous overexpression of functional membrane proteins is a major bottleneck of structural biology. Bacteriorhodopsin from Halobium salinarum (bR) is a striking example of the difficulties in membrane protein overexpression. We suggest a general approach with a finite number of steps which allows one to localize the underlying problem of poor expression of a membrane protein using bR as an example. Our approach is based on constructing chimeric proteins comprising parts of a protein of interest and complementary parts of a homologous protein demonstrating advantageous expression. This complementary protein approach allowed us to increase bR expression by two orders of magnitude through the introduction of two silent mutations into bR coding DNA. For the first time the high quality crystals of bR expressed in E. Coli were obtained using the produced protein. The crystals obtained with in meso nanovolume crystallization diffracted to 1.67 A. | ||
| - | The | + | An Approach to Heterologous Expression of Membrane Proteins. The Case of Bacteriorhodopsin.,Bratanov D, Balandin T, Round E, Shevchenko V, Gushchin I, Polovinkin V, Borshchevskiy V, Gordeliy V PLoS One. 2015 Jun 5;10(6):e0128390. doi: 10.1371/journal.pone.0128390., eCollection 2015. PMID:26046789<ref>PMID:26046789</ref> |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Balandin, T]] | ||
| + | [[Category: Bratanov, D]] | ||
[[Category: Gordeliy, V]] | [[Category: Gordeliy, V]] | ||
| - | [[Category: Balandin, T]] | ||
[[Category: Gushchin, I]] | [[Category: Gushchin, I]] | ||
| - | [[Category: Bratanov, D]] | ||
[[Category: Round, E]] | [[Category: Round, E]] | ||
| + | [[Category: Ion transport]] | ||
| + | [[Category: Proton pump]] | ||
Revision as of 12:03, 1 July 2015
Crystal Structure of Escherichia coli-Expressed Halobacterium salinarum Bacteriorhodopsin in the Trimeric Form
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