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| | <StructureSection load='1qko' size='340' side='right'caption='[[1qko]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='1qko' size='340' side='right'caption='[[1qko]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1qko]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Halobacterium_salinarium Halobacterium salinarium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QKO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QKO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1qko]] 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=1QKO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QKO FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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]] 2.1Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1qkp|1qkp]], [[1qhj|1qhj]], [[1brd|1brd]], [[2brd|2brd]], [[1brr|1brr]], [[1brx|1brx]], [[1bac|1bac]], [[1bad|1bad]], [[1bha|1bha]], [[1bhb|1bhb]], [[1bct|1bct]], [[1ap9|1ap9]], [[1at9|1at9]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qko FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qko OCA], [http://pdbe.org/1qko PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qko RCSB], [http://www.ebi.ac.uk/pdbsum/1qko PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1qko 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=1qko FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qko OCA], [https://pdbe.org/1qko PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qko RCSB], [https://www.ebi.ac.uk/pdbsum/1qko PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qko 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: Halobacterium salinarium]] | + | [[Category: Halobacterium salinarum]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Belrhali, H]] | + | [[Category: Belrhali H]] |
| - | [[Category: Edman, K]] | + | [[Category: Edman K]] |
| - | [[Category: Hajdu, J]] | + | [[Category: Hajdu J]] |
| - | [[Category: Landau, E M]] | + | [[Category: Landau EM]] |
| - | [[Category: Neutze, R]] | + | [[Category: Neutze R]] |
| - | [[Category: Nollert, P]] | + | [[Category: Nollert P]] |
| - | [[Category: Pebay-Peyroula, E]] | + | [[Category: Pebay-Peyroula E]] |
| - | [[Category: Royant, A]] | + | [[Category: Royant A]] |
| - | [[Category: Intermediate state]]
| + | |
| - | [[Category: Lipidic cubic phase]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Photocycle]]
| + | |
| - | [[Category: Photoreceptor]]
| + | |
| - | [[Category: Proton pump]]
| + | |
| - | [[Category: Retinal protein]]
| + | |
| 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
Bacteriorhodopsin is the simplest known photon-driven proton pump and as such provides a model for the study of a basic function in bioenergetics. Its seven transmembrane helices encompass a proton translocation pathway containing the chromophore, a retinal molecule covalently bound to lysine 216 through a protonated Schiff base, and a series of proton donors and acceptors. Photoisomerization of the all-trans retinal to the 13-cis configuration initiates the vectorial translocation of a proton from the Schiff base, the primary proton donor, to the extracellular side, followed by reprotonation of the Schiff base from the cytoplasm. Here we describe the high-resolution X-ray structure of an early intermediate in the photocycle of bacteriorhodopsin, which is formed directly after photoexcitation. A key water molecule is dislocated, allowing the primary proton acceptor, Asp 85, to move. Movement of the main-chain Lys 216 locally disrupts the hydrogen-bonding network of helix G, facilitating structural changes later in the photocycle.
High-resolution X-ray structure of an early intermediate in the bacteriorhodopsin photocycle.,Edman K, Nollert P, Royant A, Belrhali H, Pebay-Peyroula E, Hajdu J, Neutze R, Landau EM Nature. 1999 Oct 21;401(6755):822-6. PMID:10548112[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Edman K, Nollert P, Royant A, Belrhali H, Pebay-Peyroula E, Hajdu J, Neutze R, Landau EM. High-resolution X-ray structure of an early intermediate in the bacteriorhodopsin photocycle. Nature. 1999 Oct 21;401(6755):822-6. PMID:10548112 doi:10.1038/44623
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