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==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=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3vvk]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Natronomonas_pharaonis Natronomonas pharaonis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VVK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VVK FirstGlance]. <br> | |||
</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='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> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Halorhodopsin 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<ref>PMID:23442859</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
==See Also== | |||
*[[Bacteriorhodopsin|Bacteriorhodopsin]] | |||
*[[Rhodopsin|Rhodopsin]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Natronomonas pharaonis]] | [[Category: Natronomonas pharaonis]] | ||
[[Category: Kouyama, T | [[Category: Kouyama, T]] | ||
[[Category: Nakanishi, T | [[Category: Nakanishi, T]] | ||
[[Category: Azide-bound purple form]] | [[Category: Azide-bound purple form]] | ||
[[Category: Chloride-bound purple form]] | [[Category: Chloride-bound purple form]] | ||
Revision as of 12:25, 4 January 2015
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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