1s8l: Difference between revisions
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<StructureSection load='1s8l' size='340' side='right'caption='[[1s8l]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='1s8l' size='340' side='right'caption='[[1s8l]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1s8l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1s8l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Halobacterium_sp. Halobacterium sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S8L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S8L FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LI1:1-[2,6,10.14-TETRAMETHYL-HEXADECAN-16-YL]-2-[2,10,14-TRIMETHYLHEXADECAN-16-YL]GLYCEROL'>LI1</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=1s8l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s8l OCA], [https://pdbe.org/1s8l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s8l RCSB], [https://www.ebi.ac.uk/pdbsum/1s8l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s8l ProSAT]</span></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=1s8l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s8l OCA], [https://pdbe.org/1s8l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s8l RCSB], [https://www.ebi.ac.uk/pdbsum/1s8l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s8l ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/BACR_HALSA BACR_HALSA] Light-driven proton pump. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Halobacterium sp]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Baliga | [[Category: Baliga NS]] | ||
[[Category: Cheung | [[Category: Cheung VS]] | ||
[[Category: Facciotti | [[Category: Facciotti MT]] | ||
[[Category: Glaeser | [[Category: Glaeser RM]] | ||
[[Category: Lunde | [[Category: Lunde CS]] | ||
[[Category: Rouhani | [[Category: Rouhani S]] | ||
Latest revision as of 09:14, 23 August 2023
Anion-free form of the D85S mutant of bacteriorhodopsin from crystals grown in the presence of halideAnion-free form of the D85S mutant of bacteriorhodopsin from crystals grown in the presence of halide
Structural highlights
FunctionBACR_HALSA Light-driven proton pump. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe structure of the D85S mutant of bacteriorhodopsin with a nitrate anion bound in the Schiff base binding site and the structure of the anion-free protein have been obtained in the same crystal form. Together with the previously solved structures of this anion pump, in both the anion-free state and bromide-bound state, these new structures provide insight into how this mutant of bacteriorhodopsin is able to bind a variety of different anions in the same binding pocket. The structural analysis reveals that the main structural change that accommodates different anions is the repositioning of the polar side chain of S85. On the basis of these X-ray crystal structures, the prediction is then made that the D85S/D212N double mutant might bind similar anions and do so over a broader pH range than does the single mutant. Experimental comparison of the dissociation constants, K(d), for a variety of anions confirms this prediction and demonstrates, in addition, that the binding affinity is dramatically improved by the D212N substitution. Specificity of anion binding in the substrate pocket of bacteriorhodopsin.,Facciotti MT, Cheung VS, Lunde CS, Rouhani S, Baliga NS, Glaeser RM Biochemistry. 2004 May 4;43(17):4934-43. PMID:15109251[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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