3vvk: Difference between revisions
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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 [https://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 [https://proteopedia.org/fgij/fg.htm?mol=3VVK FirstGlance]. <br> | |||
</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3vvk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vvk OCA], [https://pdbe.org/3vvk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vvk RCSB], [https://www.ebi.ac.uk/pdbsum/3vvk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vvk ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/BACH_NATPH BACH_NATPH] Light-driven anion pump. Binding affinity for the anions is in the order, bromide > chloride > nitrate > azide > bromate and binding is pH dependent. | |||
<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> | |||
<div class="pdbe-citations 3vvk" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Bacteriorhodopsin 3D structures|Bacteriorhodopsin 3D structures]] | |||
*[[Rhodopsin 3D structures|Rhodopsin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Natronomonas pharaonis]] | |||
[[Category: Kouyama T]] | |||
[[Category: Nakanishi T]] | |||
Latest revision as of 15:39, 8 November 2023
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
FunctionBACH_NATPH Light-driven anion pump. Binding affinity for the anions is in the order, bromide > chloride > nitrate > azide > bromate and binding is pH dependent. 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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