3vvk: Difference between revisions
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==An M-like Reaction State of the azide-bound purple form of pharaonis halorhodopsin== | ==An M-like Reaction State of the azide-bound purple form of pharaonis halorhodopsin== | ||
<StructureSection load='3vvk' size='340' side='right' caption='[[3vvk]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='3vvk' size='340' side='right' caption='[[3vvk]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=22B:BACTERIORUBERIN'>22B</scene>, <scene name='pdbligand=AZI:AZIDE+ION'>AZI</scene>, <scene name='pdbligand=BNG:B-NONYLGLUCOSIDE'>BNG</scene>, <scene name='pdbligand=L3P:2,3-DI-O-PHYTANLY-3-SN-GLYCERO-1-PHOSPHORYL-3-SN-GLYCEROL-1-PHOSPHATE'>L3P</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=22B:BACTERIORUBERIN'>22B</scene>, <scene name='pdbligand=AZI:AZIDE+ION'>AZI</scene>, <scene name='pdbligand=BNG:B-NONYLGLUCOSIDE'>BNG</scene>, <scene name='pdbligand=L3P:2,3-DI-O-PHYTANLY-3-SN-GLYCERO-1-PHOSPHORYL-3-SN-GLYCEROL-1-PHOSPHATE'>L3P</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">[[3a7k|3a7k]], [[3qbi|3qbi]], [[3qbk|3qbk]], [[3qbl|3qbl]], [[3abw|3abw]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3a7k|3a7k]], [[3qbi|3qbi]], [[3qbk|3qbk]], [[3qbl|3qbl]], [[3abw|3abw]]</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=3vvk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vvk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vvk RCSB], [http://www.ebi.ac.uk/pdbsum/3vvk PDBsum]</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=3vvk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vvk OCA], [http://pdbe.org/3vvk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3vvk RCSB], [http://www.ebi.ac.uk/pdbsum/3vvk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3vvk ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3vvk" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
Revision as of 17:21, 11 August 2016
An M-like Reaction State of the azide-bound purple form of pharaonis halorhodopsinAn M-like Reaction State of the azide-bound purple form of pharaonis halorhodopsin
Structural highlights
Publication Abstract from PubMedHalorhodopsin from Natronomonas pharaonis (pHR), a retinylidene protein that functions as a light-driven chloride ion pump, is converted into a proton pump in the presence of azide ion. To clarify this conversion, we investigated light-induced structural changes in pHR using a C2 crystal that was prepared in the presence of Cl(-) and subsequently soaked in a solution containing azide ion. When the pHR-azide complex was illuminated at pH 9, a profound outward movement ( approximately 4 A) of the cytoplasmic half of helix F was observed in a subunit with the EF loop facing an open space. This movement created a long water channel between the retinal Schiff base and the cytoplasmic surface, along which a proton could be transported. Meanwhile, the middle moiety of helix C moved inward, leading to shrinkage of the primary anion-binding site (site I), and the azide molecule in site I was expelled out to the extracellular medium. The results suggest that the cytoplasmic half of helix F and the middle moiety of helix C act as different types of valves for active proton transport. Large deformation of helix F during the photoreaction cycle of Pharaonis halorhodopsin in complex with azide.,Nakanishi T, Kanada S, Murakami M, Ihara K, Kouyama T Biophys J. 2013 Jan 22;104(2):377-85. doi: 10.1016/j.bpj.2012.12.018. PMID:23442859[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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