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| Typ | Amount | VAT | Currency | Share | Status | Cost centre |
| APC | 3000.00 | 0.00 | EUR | 75.36 % | (Zahlung erfolgt) | ZB |
| APC | 981.00 | 0.00 | EUR | 24.64 % | (Zahlung erfolgt) | 44800 / E.42500.18 |
| Sum | 3981.00 | 0.00 | EUR | |||
| Total | 3981.00 |
| Journal Article | FZJ-2026-02516 |
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2026
Assoc.
Washington, DC [u.a.]
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Please use a persistent id in citations: doi:10.1126/sciadv.aed8943
Abstract: Photoreceptor sensory histidine kinases (SHKs) couple light absorption to conformational changes regulating two-component signaling. Despite their importance and widespread use in optogenetics, the underlying structural signaling mechanisms remain poorly understood. Here, we engineered dimeric SHKs based on Pseudomonas putida short light-oxygen-voltage (LOV) proteins, determined their crystal structures, and investigated their signaling mechanisms. Regardless of illumination, the structures adopted a light-state like LOV-LOV dimer with symmetric/straight kinase modules. In contrast, small-angle x-ray scattering together with functional assays revealed pronounced light-dependent rearrangements in solution and allowed the assignment of the kinase-ON dark state to an asymmetric/kinked conformation, whereas the light state adopts a symmetric/straight structure. Comparative analyses of natural and engineered SHKs identified conserved motifs linking light-induced LOV domain rotation to kinase activity. The findings highlight the central role of dimer asymmetry and flexibility in SHK signaling, thereby not least informing the engineering of new light-responsive signaling systems.
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