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| <StructureSection load='5itc' size='340' side='right'caption='[[5itc]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='5itc' size='340' side='right'caption='[[5itc]], [[Resolution|resolution]] 2.00Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[5itc]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Halwd Halwd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ITC OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5ITC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5itc]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Haloquadratum_walsbyi_DSM_16790 Haloquadratum walsbyi DSM 16790]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ITC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ITC FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=OLB:(2S)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLB</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene>, <scene name='pdbligand=RET:RETINAL'>RET</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.999Å</td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ite|5ite]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=OLB:(2S)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLB</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene>, <scene name='pdbligand=RET:RETINAL'>RET</scene></td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bop1, bopI, HQ_1014A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=362976 HALWD])</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=5itc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5itc OCA], [https://pdbe.org/5itc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5itc RCSB], [https://www.ebi.ac.uk/pdbsum/5itc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5itc ProSAT]</span></td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5itc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5itc OCA], [http://pdbe.org/5itc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5itc RCSB], [http://www.ebi.ac.uk/pdbsum/5itc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5itc ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[http://www.uniprot.org/uniprot/BACR1_HALWD BACR1_HALWD]] Light-driven proton pump. The chromophore contains 78% all-trans- and 22% 13-cis-retinal in the dark and 90% all-trans- and 10% 13-cis-retinal upon illumination with >500 nm light.<ref>PMID:21135094</ref> <ref>PMID:22248212</ref> <ref>PMID:23720753</ref> | + | [https://www.uniprot.org/uniprot/BACR1_HALWD BACR1_HALWD] Light-driven proton pump. The chromophore contains 78% all-trans- and 22% 13-cis-retinal in the dark and 90% all-trans- and 10% 13-cis-retinal upon illumination with >500 nm light.<ref>PMID:21135094</ref> <ref>PMID:22248212</ref> <ref>PMID:23720753</ref> |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Halwd]] | + | [[Category: Haloquadratum walsbyi DSM 16790]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Broecker, J]] | + | [[Category: Broecker J]] |
- | [[Category: Eger, B T]] | + | [[Category: Eger BT]] |
- | [[Category: Ernst, O P]] | + | [[Category: Ernst OP]] |
- | [[Category: Bacteriorhodopsin from haloquadratum walsbyi]]
| + | |
- | [[Category: Detergent-free]]
| + | |
- | [[Category: Lipidic cubic phase]]
| + | |
- | [[Category: Membrane protein]]
| + | |
| Structural highlights
Function
BACR1_HALWD Light-driven proton pump. The chromophore contains 78% all-trans- and 22% 13-cis-retinal in the dark and 90% all-trans- and 10% 13-cis-retinal upon illumination with >500 nm light.[1] [2] [3]
Publication Abstract from PubMed
For some membrane proteins, detergent-mediated solubilization compromises protein stability and functionality, often impairing biophysical and structural analyses. Hence, membrane-protein structure determination is a continuing bottleneck in the field of protein crystallography. Here, as an alternative to approaches mediated by conventional detergents, we report the crystallogenesis of a recombinantly produced membrane protein that never left a lipid bilayer environment. We used styrene-maleic acid (SMA) copolymers to solubilize lipid-embedded proteins into SMA nanodiscs, purified these discs by affinity and size-exclusion chromatography, and transferred proteins into the lipidic cubic phase (LCP) for in meso crystallization. The 2.0-A structure of an alpha-helical seven-transmembrane microbial rhodopsin thus obtained is of high quality and virtually identical to the 2.2-A structure obtained from traditional detergent-based purification and subsequent LCP crystallization.
Crystallogenesis of Membrane Proteins Mediated by Polymer-Bounded Lipid Nanodiscs.,Broecker J, Eger BT, Ernst OP Structure. 2017 Jan 3. pii: S0969-2126(16)30394-X. doi:, 10.1016/j.str.2016.12.004. PMID:28089451[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Sudo Y, Ihara K, Kobayashi S, Suzuki D, Irieda H, Kikukawa T, Kandori H, Homma M. A microbial rhodopsin with a unique retinal composition shows both sensory rhodopsin II and bacteriorhodopsin-like properties. J Biol Chem. 2011 Feb 25;286(8):5967-76. doi: 10.1074/jbc.M110.190058. Epub 2010 , Dec 6. PMID:21135094 doi:http://dx.doi.org/10.1074/jbc.M110.190058
- ↑ Lobasso S, Lopalco P, Vitale R, Saponetti MS, Capitanio G, Mangini V, Milano F, Trotta M, Corcelli A. The light-activated proton pump Bop I of the archaeon Haloquadratum walsbyi. Photochem Photobiol. 2012 May-Jun;88(3):690-700. doi:, 10.1111/j.1751-1097.2012.01089.x. Epub 2012 Feb 9. PMID:22248212 doi:http://dx.doi.org/10.1111/j.1751-1097.2012.01089.x
- ↑ Sudo Y, Okazaki A, Ono H, Yagasaki J, Sugo S, Kamiya M, Reissig L, Inoue K, Ihara K, Kandori H, Takagi S, Hayashi S. A blue-shifted light-driven proton pump for neural silencing. J Biol Chem. 2013 Jul 12;288(28):20624-32. doi: 10.1074/jbc.M113.475533. Epub, 2013 May 28. PMID:23720753 doi:http://dx.doi.org/10.1074/jbc.M113.475533
- ↑ Broecker J, Eger BT, Ernst OP. Crystallogenesis of Membrane Proteins Mediated by Polymer-Bounded Lipid Nanodiscs. Structure. 2017 Jan 3. pii: S0969-2126(16)30394-X. doi:, 10.1016/j.str.2016.12.004. PMID:28089451 doi:http://dx.doi.org/10.1016/j.str.2016.12.004
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