Author
Listed:
- Robert Bosman
(University of Gothenburg)
- Giorgia Ortolani
(University of Gothenburg)
- Swagatha Ghosh
(University of Gothenburg)
- Daniel James
(Forschungsstrasse 111)
- Per Norder
(University of Gothenburg)
- Greger Hammarin
(University of Gothenburg)
- Tinna Björg Úlfarsdóttir
(University of Gothenburg)
- Lucija Ostojić
(University of Gothenburg)
- Tobias Weinert
(Forschungsstrasse 111)
- Florian Dworkowski
(Forschungsstrasse 111)
- Takashi Tomizaki
(Forschungsstrasse 111)
- Jörg Standfuss
(Forschungsstrasse 111)
- Gisela Brändén
(University of Gothenburg)
- Richard Neutze
(University of Gothenburg)
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.
Suggested Citation
Robert Bosman & Giorgia Ortolani & Swagatha Ghosh & Daniel James & Per Norder & Greger Hammarin & Tinna Björg Úlfarsdóttir & Lucija Ostojić & Tobias Weinert & Florian Dworkowski & Takashi Tomizaki & J, 2025.
"Structural basis for the prolonged photocycle of sensory rhodopsin II revealed by serial synchrotron crystallography,"
Nature Communications, Nature, vol. 16(1), pages 1-12, December.
Handle:
RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-58263-x
DOI: 10.1038/s41467-025-58263-x
Download full text from publisher
Corrections
All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-58263-x. See general information about how to correct material in RePEc.
If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.
We have no bibliographic references for this item. You can help adding them by using this form .
If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.
For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .
Please note that corrections may take a couple of weeks to filter through
the various RePEc services.