8AVV

Cryo-EM structure of DrBphP photosensory module in Pr state

8AVV の概要

• エントリーDOI: 10.2210/pdb8avv/pdb
• EMDBエントリー: 15684
• 分子名称: Bacteriophytochrome,Response regulator, 3-[2-[(Z)-[3-(2-carboxyethyl)-5-[(Z)-(4-ethenyl-3-methyl-5-oxidanylidene-pyrrol-2-ylidene)methyl]-4-methyl-pyrrol-1-ium -2-ylidene]methyl]-5-[(Z)-[(3E)-3-ethylidene-4-methyl-5-oxidanylidene-pyrrolidin-2-ylidene]methyl]-4-methyl-1H-pyrrol-3- yl]propanoic acid (2 entities in total)
• 機能のキーワード: kinase, photosensor, transferase, phytochrome
• 由来する生物種: Deinococcus radiodurans R1; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 204329.67

構造登録者

Wahlgren, W.Y.,Takala, H.,Westenhoff, S. (登録日: 2022-08-27, 公開日: 2022-12-21, 最終更新日: 2024-07-24)

主引用文献

Wahlgren, W.Y.,Claesson, E.,Tuure, I.,Trillo-Muyo, S.,Bodizs, S.,Ihalainen, J.A.,Takala, H.,Westenhoff, S.
Structural mechanism of signal transduction in a phytochrome histidine kinase.
Nat Commun, 13:7673-7673, 2022

PubMed Abstract: 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 Å and 3.5 Å 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.

PubMed: 36509762
DOI: 10.1038/s41467-022-34893-3

実験手法

ELECTRON MICROSCOPY (3.4 Å)