8UPM

Pfr state of Stigmatella aurantiaca bacteriophytochrome 2

8UPM の概要

• エントリーDOI: 10.2210/pdb8upm/pdb
• EMDBエントリー: 42452
• 分子名称: Bacteriophytochrome (Light-regulated signal transduction histidine kinase), BILIVERDINE IX ALPHA (2 entities in total)
• 機能のキーワード: red light photoreceptor, two component system, signaling protein
• 由来する生物種: Stigmatella aurantiaca
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 163466.81

構造登録者

Malla, T.N.,Schmidt, M.,Stojkovic, E.A. (登録日: 2023-10-23, 公開日: 2024-09-25, 最終更新日: 2024-11-06)

主引用文献

Malla, T.N.,Hernandez, C.,Muniyappan, S.,Menendez, D.,Bizhga, D.,Mendez, J.H.,Schwander, P.,Stojkovic, E.A.,Schmidt, M.
Photoreception and signaling in bacterial phytochrome revealed by single-particle cryo-EM.
Sci Adv, 10:eadq0653-eadq0653, 2024

PubMed Abstract: Phytochromes are red-light photoreceptors discovered in plants with homologs in bacteria and fungi that regulate a variety of physiological responses. They display a reversible photocycle between two distinct states: a red-light-absorbing Pr state and a far-red light-absorbing Pfr state. The photoconversion regulates the activity of an enzymatic domain, usually a histidine kinase (HK). The molecular mechanism that explains how light controls the HK activity is not understood because structures of unmodified bacterial phytochromes with HK activity are missing. Here, we report three cryo-electron microscopy structures of a wild-type bacterial phytochrome with HK activity determined as Pr and Pfr homodimers and as a Pr/Pfr heterodimer with individual subunits in distinct states. We propose that the Pr/Pfr heterodimer is a physiologically relevant signal transduction intermediate. Our results offer insight into the molecular mechanism that controls the enzymatic activity of the HK as part of a bacterial two-component system that perceives and transduces light signals.

PubMed: 39121216
DOI: 10.1126/sciadv.adq0653

実験手法

ELECTRON MICROSCOPY (3.75 Å)