9h1x
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Continuously illuminated structure of Sensory Rhodopsin II solved by serial millisecond crystallography== | |
| + | <StructureSection load='9h1x' size='340' side='right'caption='[[9h1x]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[9h1x]] is a 1 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=9H1X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9H1X 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]] 1.85Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=9h1x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9h1x OCA], [https://pdbe.org/9h1x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9h1x RCSB], [https://www.ebi.ac.uk/pdbsum/9h1x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9h1x ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/BACS2_NATPH BACS2_NATPH] Involved in the control of phototaxis. Seems to activate a methyl-accepting protein (HTR-II). Photoreceptor for blue light. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Microbial rhodopsins form a diverse family of light-sensitive seven-transmembrane helix retinal proteins that function as active proton or ion pumps, passive light-gated ion channels, and photosensors. To understand how light-sensing in archaea is initiated by sensory rhodopsins, we perform serial synchrotron X-ray crystallography (SSX) studies of light induced conformational changes in sensory rhodopsin II (NpSRII) from the archaea Natronomonas pharaonis, both collecting time-resolved SSX data and collecting SSX data during continuous illumination. Comparing light-induced electron density changes in NpSRII with those reported for bacteriorhodopsin (bR) reveals several common light-induced structural perturbations. Unlike bR, however, helix G of NpSRII does not unwind near the conserved lysine residue to which retinal is covalently bound and therefore transient water molecule binding sites do not arise immediately to the cytoplasmic side of retinal. These structural differences prolong the duration of the NpSRII photocycle relative to bR, allowing time for the light-initiated sensory signal to be amplified. | ||
| - | + | Structural basis for the prolonged photocycle of sensory rhodopsin II revealed by serial synchrotron crystallography.,Bosman R, Ortolani G, Ghosh S, James D, Norder P, Hammarin G, Ulfarsdottir TB, Ostojic L, Weinert T, Dworkowski F, Tomizaki T, Standfuss J, Branden G, Neutze R Nat Commun. 2025 Apr 11;16(1):3460. doi: 10.1038/s41467-025-58263-x. PMID:40216733<ref>PMID:40216733</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 9h1x" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Natronomonas pharaonis]] | ||
| + | [[Category: Bosman R]] | ||
| + | [[Category: Branden G]] | ||
| + | [[Category: Neutze R]] | ||
| + | [[Category: Ortolani G]] | ||
Current revision
Continuously illuminated structure of Sensory Rhodopsin II solved by serial millisecond crystallography
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