Conserved histidine and tyrosine determine spectral responses through the water network in Deinococcus radiodurans phytochrome
Lehtivuori, H., Rumfeldt, J., Mustalahti, S., Kurkinen, S., & Takala, H. (2022). Conserved histidine and tyrosine determine spectral responses through the water network in Deinococcus radiodurans phytochrome. Photochemical and Photobiological Sciences, 21(11), 1975-1989. https://doi.org/10.1007/s43630-022-00272-6
Julkaistu sarjassa
Photochemical and Photobiological SciencesPäivämäärä
2022Oppiaine
Solu- ja molekyylibiologiaNanoscience CenterFysikaalinen kemiaFysiikkaCell and Molecular BiologyNanoscience CenterPhysical ChemistryPhysicsTekijänoikeudet
© The Author(s) 2022
Phytochromes are red light-sensing photoreceptor proteins that bind a bilin chromophore. Here, we investigate the role of a conserved histidine (H260) and tyrosine (Y263) in the chromophore-binding domain (CBD) of Deinococcus radiodurans phytochrome (DrBphP). Using crystallography, we show that in the H260A variant, the missing imidazole side chain leads to increased water content in the binding pocket. On the other hand, Y263F mutation reduces the water occupancy around the chromophore. Together, these changes in water coordination alter the protonation and spectroscopic properties of the biliverdin. These results pinpoint the importance of this conserved histidine and tyrosine, and the related water network, for the function and applications of phytochromes.
Julkaisija
Springer Science and Business Media LLCISSN Hae Julkaisufoorumista
1474-905XAsiasanat
Julkaisu tutkimustietojärjestelmässä
https://converis.jyu.fi/converis/portal/detail/Publication/150995821
Metadata
Näytä kaikki kuvailutiedotKokoelmat
Rahoittaja(t)
Suomen AkatemiaRahoitusohjelmat(t)
Akatemiahanke, SA; Akatemiatutkija, SA; Tutkijatohtori, SALisätietoja rahoituksesta
This work was supported by Academy of Finland grants 285461 (H.T.), 330678 (H.T., J.R.), 277194 (H.L.), and 290677 (S.M.).Lisenssi
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