6XVU

Bacteriophytochrome response regulator from Deinococcus radiodurans

6XVU の概要

• エントリーDOI: 10.2210/pdb6xvu/pdb
• 分子名称: Response regulator, CALCIUM ION (3 entities in total)
• 機能のキーワード: response regulator, two-component system, signaling protein
• 由来する生物種: Deinococcus radiodurans R1
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 76639.58

構造登録者

Takala, H.,Ihalainen, J.A. (登録日: 2020-01-22, 公開日: 2021-06-30, 最終更新日: 2024-01-24)

主引用文献

Multamaki, E.,Nanekar, R.,Morozov, D.,Lievonen, T.,Golonka, D.,Wahlgren, W.Y.,Stucki-Buchli, B.,Rossi, J.,Hytonen, V.P.,Westenhoff, S.,Ihalainen, J.A.,Moglich, A.,Takala, H.
Comparative analysis of two paradigm bacteriophytochromes reveals opposite functionalities in two-component signaling.
Nat Commun, 12:4394-4394, 2021

PubMed Abstract: Bacterial phytochrome photoreceptors usually belong to two-component signaling systems which transmit environmental stimuli to a response regulator through a histidine kinase domain. Phytochromes switch between red light-absorbing and far-red light-absorbing states. Despite exhibiting extensive structural responses during this transition, the model bacteriophytochrome from Deinococcus radiodurans (DrBphP) lacks detectable kinase activity. Here, we resolve this long-standing conundrum by comparatively analyzing the interactions and output activities of DrBphP and a bacteriophytochrome from Agrobacterium fabrum (Agp1). Whereas Agp1 acts as a conventional histidine kinase, we identify DrBphP as a light-sensitive phosphatase. While Agp1 binds its cognate response regulator only transiently, DrBphP does so strongly, which is rationalized at the structural level. Our data pinpoint two key residues affecting the balance between kinase and phosphatase activities, which immediately bears on photoreception and two-component signaling. The opposing output activities in two highly similar bacteriophytochromes suggest the use of light-controllable histidine kinases and phosphatases for optogenetics.

PubMed: 34285211
DOI: 10.1038/s41467-021-24676-7

実験手法

X-RAY DIFFRACTION (2.1 Å)