Time-resolved X-ray solution scattering observations of light-induced structural changes in sensory rhodopsin II

Unicellular organisms respond to a changing environment through physical and chemical sensory cascades. Sensory rhodopsin II (SRII) is a blue-light receptor, which initiates a negative phototaxis response in the host archaea. Here, we apply time-resolved X-ray solution scattering (TR-XSS) to characterize the mechanism of signal transduction by SRII and explore how light-induced structural changes are modified when SRII is in complex with its transducer protein (HtrII). TR-XSS difference data are modeled as arising from an outward movement of helices E and F in combination with modest changes associated with helices C and the extracellular regions of helices D and E. The magnitude of the displacement of helices E and F is similar irrespective of whether or not HtrII is present. In combination with structural predictions of the full SRII:HtrII complex, TR-XSS provides insight into how conformational changes may be communicated from SRII to the signaling domain of HtrII.

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Publication Details

Journal
Structure
Published
2026-01-26
DOI
https://doi.org/10.1016/j.str.2025.12.014
Primary Topic
Photoreceptor and optogenetics research
Type
article
Field-Weighted Citation Impact
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article

Time-resolved X-ray solution scattering observations of light-induced structural changes in sensory rhodopsin II

Robert Bosman, Martin Nors Pedersen, Richard Neutze, Swagatha Ghosh et al.
Structure
Photoreceptor and optogenetics research
article

Time-resolved X-ray solution scattering observations of light-induced structural changes in sensory rhodopsin II

Robert Bosman, Martin Nors Pedersen, Richard Neutze, Swagatha Ghosh, M. Wulff, Robert Dods, Daniel Sarabi, Giorgia Ortolani, Mathias Sander, Greger Hammarin, Lucija Ostojić, Gisela Brändén, Cecilia Safari, Petra Båth, Per Norder, Matteo Levantino
article en

Abstract

Unicellular organisms respond to a changing environment through physical and chemical sensory cascades. Sensory rhodopsin II (SRII) is a blue-light receptor, which initiates a negative phototaxis response in the host archaea. Here, we apply time-resolved X-ray solution scattering (TR-XSS) to characterize the mechanism of signal transduction by SRII and explore how light-induced structural changes are modified when SRII is in complex with its transducer protein (HtrII). TR-XSS difference data are modeled as arising from an outward movement of helices E and F in combination with modest changes associated with helices C and the extracellular regions of helices D and E. The magnitude of the displacement of helices E and F is similar irrespective of whether or not HtrII is present. In combination with structural predictions of the full SRII:HtrII complex, TR-XSS provides insight into how conformational changes may be communicated from SRII to the signaling domain of HtrII.

StructureVol. 34(3)
European Synchrotron Radiation Facility (FR), University of Gothenburg (SE)
Openalex Percentile: Top 79%
Photoreceptor and optogenetics research
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