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7JR5

Real Time Reaction Intermediates in Stigmatella Bacteriophytochrome P2

Summary for 7JR5
Entry DOI10.2210/pdb7jr5/pdb
DescriptorPhotoreceptor-histidine kinase BphP, 3-[2-[[5-[(4-ethenyl-3-methyl-5-oxidanylidene-pyrrol-2-yl)methyl]-3-(3-hydroxy-3-oxopropyl)-4-methyl-1~{H}-pyrrol-2-yl]methyl]-5-[[(3~{S})-4-ethyl-3-methyl-2-oxidanylidene-1,3-dihydropyrrol-5-yl]methyl]-4-methyl-1~{H}-pyrrol-3-yl]propanoic acid, BENZAMIDINE, ... (4 entities in total)
Functional Keywordsphytochrome, photosensory core domain, time-resolved serial femtosecond crystallography, nanosecond, red/far-red, z to e isomerization, signaling protein
Biological sourceStigmatella aurantiaca (strain DW4/3-1)
Total number of polymer chains2
Total formula weight106942.52
Authors
Schmidt, M. (deposition date: 2020-08-11, release date: 2021-10-06, Last modification date: 2024-10-16)
Primary citationCarrillo, M.,Pandey, S.,Sanchez, J.,Noda, M.,Poudyal, I.,Aldama, L.,Malla, T.N.,Claesson, E.,Wahlgren, W.Y.,Feliz, D.,Srajer, V.,Maj, M.,Castillon, L.,Iwata, S.,Nango, E.,Tanaka, R.,Tanaka, T.,Fangjia, L.,Tono, K.,Owada, S.,Westenhoff, S.,Stojkovic, E.A.,Schmidt, M.
High-resolution crystal structures of transient intermediates in the phytochrome photocycle.
Structure, 29:743-754.e4, 2021
Cited by
PubMed Abstract: Phytochromes are red/far-red light photoreceptors in bacteria to plants, which elicit a variety of important physiological responses. They display a reversible photocycle between the resting Pr state and the light-activated Pfr state. Light signals are transduced as structural change through the entire protein to modulate its activity. It is unknown how the Pr-to-Pfr interconversion occurs, as the structure of intermediates remains notoriously elusive. Here, we present short-lived crystal structures of the photosensory core modules of the bacteriophytochrome from myxobacterium Stigmatella aurantiaca captured by an X-ray free electron laser 5 ns and 33 ms after light illumination of the Pr state. We observe large structural displacements of the covalently bound bilin chromophore, which trigger a bifurcated signaling pathway that extends through the entire protein. The snapshots show with atomic precision how the signal progresses from the chromophore, explaining how plants, bacteria, and fungi sense red light.
PubMed: 33756101
DOI: 10.1016/j.str.2021.03.004
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.4 Å)
Structure validation

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