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| | <StructureSection load='1o0a' size='340' side='right'caption='[[1o0a]], [[Resolution|resolution]] 1.62Å' scene=''> | | <StructureSection load='1o0a' size='340' side='right'caption='[[1o0a]], [[Resolution|resolution]] 1.62Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1o0a]] is a 1 chain structure with sequence from [http://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=1O0A OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1O0A FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1o0a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Halobacterium_salinarum Halobacterium salinarum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O0A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O0A FirstGlance]. <br> |
| - | </td></tr><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>, <scene name='pdbligand=SQU:2,10,23-TRIMETHYL-TETRACOSANE'>SQU</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]] 1.62Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1c3w|1c3w]], [[1m0l|1m0l]], [[1m0k|1m0k]], [[1m0m|1m0m]]</div></td></tr>
| + | <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>, <scene name='pdbligand=SQU:2,10,23-TRIMETHYL-TETRACOSANE'>SQU</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BOP ([http://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=1o0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o0a OCA], [https://pdbe.org/1o0a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o0a RCSB], [https://www.ebi.ac.uk/pdbsum/1o0a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o0a 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=1o0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o0a OCA], [http://pdbe.org/1o0a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1o0a RCSB], [http://www.ebi.ac.uk/pdbsum/1o0a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1o0a ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/BACR_HALSA BACR_HALSA]] Light-driven proton pump. | + | [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: Bacillus halobius ruber klebahn 1919]] | + | [[Category: Halobacterium salinarum]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lanyi, J K]] | + | [[Category: Lanyi JK]] |
| - | [[Category: 7-transmembrane]]
| + | |
| - | [[Category: Haloarchaea]]
| + | |
| - | [[Category: Ion pump]]
| + | |
| - | [[Category: Lipid]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Merohedral twinning]]
| + | |
| - | [[Category: Photoreceptor]]
| + | |
| - | [[Category: Proton transport]]
| + | |
| - | [[Category: Retinal protein]]
| + | |
| - | [[Category: Serpentine]]
| + | |
| Structural highlights
Function
BACR_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 PubMed
We produced the L intermediate of the photocycle in a bacteriorhodopsin crystal in photo-stationary state at 170 K with red laser illumination at 60% occupancy, and determined its structure to 1.62 A resolution. With this model, high-resolution structural information is available for the initial bacteriorhodopsin, as well as the first five states in the transport cycle. These states involve photo-isomerization of the retinal and its initial configurational changes, deprotonation of the retinal Schiff base and the coupled release of a proton to the extracellular membrane surface, and the switch event that allows reprotonation of the Schiff base from the cytoplasmic side. The six structural models describe the transformations of the retinal and its interaction with water 402, Asp85, and Asp212 in atomic detail, as well as the displacements of functional residues farther from the Schiff base. The changes provide rationales for how relaxation of the distorted retinal causes movements of water and protein atoms that result in vectorial proton transfers to and from the Schiff base.
Mechanism of proton transport in bacteriorhodopsin from crystallographic structures of the K, L, M1, M2, and M2' intermediates of the photocycle.,Lanyi JK, Schobert B J Mol Biol. 2003 Apr 25;328(2):439-50. PMID:12691752[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lanyi JK, Schobert B. Mechanism of proton transport in bacteriorhodopsin from crystallographic structures of the K, L, M1, M2, and M2' intermediates of the photocycle. J Mol Biol. 2003 Apr 25;328(2):439-50. PMID:12691752
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