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| <StructureSection load='5b0w' size='340' side='right'caption='[[5b0w]], [[Resolution|resolution]] 1.70Å' scene=''> | | <StructureSection load='5b0w' size='340' side='right'caption='[[5b0w]], [[Resolution|resolution]] 1.70Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[5b0w]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Natronomonas_pharaonis_dsm_2160 Natronomonas pharaonis dsm 2160]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B0W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5B0W FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5b0w]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Natronomonas_pharaonis_DSM_2160 Natronomonas pharaonis DSM 2160]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B0W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5B0W 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=BNG:B-NONYLGLUCOSIDE'>BNG</scene>, <scene name='pdbligand=ILE:ISOLEUCINE'>ILE</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" id="ligandDat"><scene name='pdbligand=22B:BACTERIORUBERIN'>22B</scene>, <scene name='pdbligand=BNG:B-NONYLGLUCOSIDE'>BNG</scene>, <scene name='pdbligand=ILE:ISOLEUCINE'>ILE</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">[[3qbg|3qbg]]</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=5b0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b0w OCA], [https://pdbe.org/5b0w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5b0w RCSB], [https://www.ebi.ac.uk/pdbsum/5b0w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5b0w ProSAT]</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=5b0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b0w OCA], [http://pdbe.org/5b0w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5b0w RCSB], [http://www.ebi.ac.uk/pdbsum/5b0w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5b0w ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| </StructureSection> | | </StructureSection> |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Natronomonas pharaonis dsm 2160]] | + | [[Category: Natronomonas pharaonis DSM 2160]] |
- | [[Category: Chan, S K]] | + | [[Category: Chan SK]] |
- | [[Category: Kouyama, T]] | + | [[Category: Kouyama T]] |
- | [[Category: Light-driven chloride ion pump microbial rhodopsin]]
| + | |
- | [[Category: Membrane protein]]
| + | |
- | [[Category: Retinylidene protein]]
| + | |
- | [[Category: Seven trans-membrane helice]]
| + | |
| Structural highlights
Publication Abstract from PubMed
Like other microbial rhodopsins, the light driven chloride pump halorhodopsin from Natronomonas pharaonis (pHR) contains a mixture of all-trans/15-anti and 13-cis/15-syn isomers in the dark adapted state. A recent crystallographic study of the reaction states of pHR has shown that reaction states with 13-cis/15-syn retinal occur in the anion pumping cycle that is initiated by excitation of the all-trans isomer. In this study, we investigated interconversions among different isomeric states of pHR in the absence of chloride ions. The illumination of chloride free pHR with red light caused a large blue shift in the absorption maximum of the retinal visible band. During this "red adaptation", the content of the 11-cis isomer increased significantly, while the molar ratio of the 13-cis isomer to the all-trans isomer remained unchanged. The results suggest that the thermally activated interconversion between the 13-cis and the all-trans isomers is very rapid. Diffraction data from red adapted crystals showed that accommodation of the retinal chromophore with the 11-cis/15-syn configuration was achieved without a large change in the retinal binding pocket. The measurement of absorption kinetics under illumination showed that the 11-cis isomer, with a lambdamax at 565 nm, was generated upon excitation of a red-shifted species (lambdamax = 625 nm) that was present as a minor component in the dark adapted state. It is possible that this red-shifted species mimics an O-like reaction state with 13-cis/15-syn retinal, which was hypothesized to occur at a late stage of the anion pumping cycle.
Crystal Structure of the 11-cis Isomer of Pharaonis Halorhodopsin: Structural Constraints on Interconversions among Different Isomeric States.,Chan SK, Kawaguchi H, Kubo H, Murakami M, Ihara K, Maki K, Kouyama T Biochemistry. 2016 Jul 26;55(29):4092-104. doi: 10.1021/acs.biochem.6b00277. Epub, 2016 Jul 13. PMID:27352034[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Chan SK, Kawaguchi H, Kubo H, Murakami M, Ihara K, Maki K, Kouyama T. Crystal Structure of the 11-cis Isomer of Pharaonis Halorhodopsin: Structural Constraints on Interconversions among Different Isomeric States. Biochemistry. 2016 Jul 26;55(29):4092-104. doi: 10.1021/acs.biochem.6b00277. Epub, 2016 Jul 13. PMID:27352034 doi:http://dx.doi.org/10.1021/acs.biochem.6b00277
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