5ite: Difference between revisions
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<StructureSection load='5ite' size='340' side='right' caption='[[5ite]], [[Resolution|resolution]] 2.18Å' scene=''> | <StructureSection load='5ite' size='340' side='right' caption='[[5ite]], [[Resolution|resolution]] 2.18Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5ite]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ITE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ITE FirstGlance]. <br> | <table><tr><td colspan='2'>[[5ite]] 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=5ITE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ITE FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5itc|5itc]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5itc|5itc]]</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ite FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ite OCA], [http://pdbe.org/5ite PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ite RCSB], [http://www.ebi.ac.uk/pdbsum/5ite PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ite ProSAT]</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=5ite FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ite OCA], [http://pdbe.org/5ite PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ite RCSB], [http://www.ebi.ac.uk/pdbsum/5ite PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ite ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Halwd]] | |||
[[Category: Broecker, J]] | [[Category: Broecker, J]] | ||
[[Category: Eger, B T]] | [[Category: Eger, B T]] | ||
Revision as of 13:02, 22 November 2017
2.2-Angstrom in meso crystal structure of Haloquadratum Walsbyi Bacteriorhodopsin (HwBR) from Octylglucoside (OG) Detergent Micelles2.2-Angstrom in meso crystal structure of Haloquadratum Walsbyi Bacteriorhodopsin (HwBR) from Octylglucoside (OG) Detergent Micelles
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 PubMedFor 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. References
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