7Z9D

Deinococcus radiodurans BphP PAS-GAF H260A mutant

Summary for 7Z9D

• Entry DOI: 10.2210/pdb7z9d/pdb
• Related: 5K5B 5NFX
• Descriptor: Bacteriophytochrome, ACETATE ION, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (5 entities in total)
• Functional Keywords: kinase, photosensor, transferase, phytochrome
• Biological source: Deinococcus radiodurans R1
• Total number of polymer chains: 1
• Total formula weight: 38043.36

Authors

Takala, H. (deposition date: 2022-03-21, release date: 2022-08-10, Last modification date: 2024-11-13)

Primary citation

Lehtivuori, H.,Rumfeldt, J.,Mustalahti, S.,Kurkinen, S.,Takala, H.
Conserved histidine and tyrosine determine spectral responses through the water network in Deinococcus radiodurans phytochrome.
Photochem Photobiol Sci, 21:1975-1989, 2022

PubMed Abstract: 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.

PubMed: 35906527
DOI: 10.1007/s43630-022-00272-6

Experimental method

X-RAY DIFFRACTION (1.88 Å)