8avv

From Proteopedia

Cryo-EM structure of DrBphP photosensory module in Pr state

Structural highlights

8avv is a 2 chain structure with sequence from Deinococcus radiodurans R1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 3.4Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

BPHY_DEIRA Photoreceptor which exists in two forms that are reversibly interconvertible by light: the R form that absorbs maximally in the red region of the spectrum and the FR form that absorbs maximally in the far-red region. Has also a slight blue shift for the far-red maximum. Could also absorb green light. May participate in regulating pigment synthesis like the carotenoid deinoxanthin which could protect the bacterium from intense visible light.Q9RZA5_DEIRA

Publication Abstract from PubMed

Phytochrome proteins detect red/far-red light to guide the growth, motion, development and reproduction in plants, fungi, and bacteria. Bacterial phytochromes commonly function as an entrance signal in two-component sensory systems. Despite the availability of three-dimensional structures of phytochromes and other two-component proteins, the conformational changes, which lead to activation of the protein, are not understood. We reveal cryo electron microscopy structures of the complete phytochrome from Deinoccocus radiodurans in its resting and photoactivated states at 3.6 A and 3.5 A resolution, respectively. Upon photoactivation, the photosensory core module hardly changes its tertiary domain arrangement, but the connector helices between the photosensory and the histidine kinase modules open up like a zipper, causing asymmetry and disorder in the effector domains. The structures provide a framework for atom-scale understanding of signaling in phytochromes, visualize allosteric communication over several nanometers, and suggest that disorder in the dimeric arrangement of the effector domains is important for phosphatase activity in a two-component system. The results have implications for the development of optogenetic applications.

Structural mechanism of signal transduction in a phytochrome histidine kinase.,Wahlgren WY, Claesson E, Tuure I, Trillo-Muyo S, Bodizs S, Ihalainen JA, Takala H, Westenhoff S Nat Commun. 2022 Dec 12;13(1):7673. doi: 10.1038/s41467-022-34893-3. PMID:36509762^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Wahlgren WY, Claesson E, Tuure I, Trillo-Muyo S, Bódizs S, Ihalainen JA, Takala H, Westenhoff S. Structural mechanism of signal transduction in a phytochrome histidine kinase. Nat Commun. 2022 Dec 12;13(1):7673. PMID:36509762 doi:10.1038/s41467-022-34893-3