Structural basis for the prolonged photocycle of sensory rhodopsin II revealed by serial synchrotron crystallography
Abstract 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...
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Nature Portfolio
2025-04-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-025-58263-x |
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| author | Robert Bosman Giorgia Ortolani Swagatha Ghosh Daniel James Per Norder Greger Hammarin Tinna Björg Úlfarsdóttir Lucija Ostojić Tobias Weinert Florian Dworkowski Takashi Tomizaki Jörg Standfuss Gisela Brändén Richard Neutze |
| author_facet | Robert Bosman Giorgia Ortolani Swagatha Ghosh Daniel James Per Norder Greger Hammarin Tinna Björg Úlfarsdóttir Lucija Ostojić Tobias Weinert Florian Dworkowski Takashi Tomizaki Jörg Standfuss Gisela Brändén Richard Neutze |
| author_sort | Robert Bosman |
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| description | Abstract 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. |
| format | Article |
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| institution | OA Journals |
| issn | 2041-1723 |
| language | English |
| publishDate | 2025-04-01 |
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| spelling | doaj-art-b8d39a98c721407ca768780e78ecb9b22025-08-20T02:28:04ZengNature PortfolioNature Communications2041-17232025-04-0116111210.1038/s41467-025-58263-xStructural basis for the prolonged photocycle of sensory rhodopsin II revealed by serial synchrotron crystallographyRobert Bosman0Giorgia Ortolani1Swagatha Ghosh2Daniel James3Per Norder4Greger Hammarin5Tinna Björg Úlfarsdóttir6Lucija Ostojić7Tobias Weinert8Florian Dworkowski9Takashi Tomizaki10Jörg Standfuss11Gisela Brändén12Richard Neutze13Department of Chemistry and Molecular Biology, University of GothenburgDepartment of Chemistry and Molecular Biology, University of GothenburgDepartment of Chemistry and Molecular Biology, University of GothenburgLaboratory of Biomolecular Research, Center for Life Sciences, Paul Scherrer Institut, Forschungsstrasse 111Department of Chemistry and Molecular Biology, University of GothenburgDepartment of Chemistry and Molecular Biology, University of GothenburgDepartment of Chemistry and Molecular Biology, University of GothenburgDepartment of Chemistry and Molecular Biology, University of GothenburgLaboratory of Biomolecular Research, Center for Life Sciences, Paul Scherrer Institut, Forschungsstrasse 111Laboratory of Femtochemistry, Center for Photon Science, Paul Scherrer Institut, Forschungsstrasse 111Laboratory of Macromolecules and Bioimaging, Center for Photon Science, Paul Scherrer Institut, Forschungsstrasse 111Laboratory of Biomolecular Research, Center for Life Sciences, Paul Scherrer Institut, Forschungsstrasse 111Department of Chemistry and Molecular Biology, University of GothenburgDepartment of Chemistry and Molecular Biology, University of GothenburgAbstract 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.https://doi.org/10.1038/s41467-025-58263-x |
| spellingShingle | Robert Bosman Giorgia Ortolani Swagatha Ghosh Daniel James Per Norder Greger Hammarin Tinna Björg Úlfarsdóttir Lucija Ostojić Tobias Weinert Florian Dworkowski Takashi Tomizaki Jörg Standfuss Gisela Brändén Richard Neutze Structural basis for the prolonged photocycle of sensory rhodopsin II revealed by serial synchrotron crystallography Nature Communications |
| title | Structural basis for the prolonged photocycle of sensory rhodopsin II revealed by serial synchrotron crystallography |
| title_full | Structural basis for the prolonged photocycle of sensory rhodopsin II revealed by serial synchrotron crystallography |
| title_fullStr | Structural basis for the prolonged photocycle of sensory rhodopsin II revealed by serial synchrotron crystallography |
| title_full_unstemmed | Structural basis for the prolonged photocycle of sensory rhodopsin II revealed by serial synchrotron crystallography |
| title_short | Structural basis for the prolonged photocycle of sensory rhodopsin II revealed by serial synchrotron crystallography |
| title_sort | structural basis for the prolonged photocycle of sensory rhodopsin ii revealed by serial synchrotron crystallography |
| url | https://doi.org/10.1038/s41467-025-58263-x |
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