5JYU

NMR structure of pseudo receiver domain of CikA from Thermosynechococcus elongatus

5JYU の概要

• エントリーDOI: 10.2210/pdb5jyu/pdb
• 関連するPDBエントリー: 5JYT 5JYV
• NMR情報: BMRB: 30092
• 分子名称: Two-component sensor histidine kinase (1 entity in total)
• 機能のキーワード: circadian clock, signaling protein, sigaling protein
• 由来する生物種: Thermosynechococcus elongatus (strain BP-1)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12899.74

構造登録者

Tseng, R.D.,LiWang, A.L. (登録日: 2016-05-15, 公開日: 2017-03-29, 最終更新日: 2024-05-15)

主引用文献

Tseng, R.,Goularte, N.F.,Chavan, A.,Luu, J.,Cohen, S.E.,Chang, Y.G.,Heisler, J.,Li, S.,Michael, A.K.,Tripathi, S.,Golden, S.S.,LiWang, A.,Partch, C.L.
Structural basis of the day-night transition in a bacterial circadian clock.
Science, 355:1174-1180, 2017

PubMed Abstract: Circadian clocks are ubiquitous timing systems that induce rhythms of biological activities in synchrony with night and day. In cyanobacteria, timing is generated by a posttranslational clock consisting of KaiA, KaiB, and KaiC proteins and a set of output signaling proteins, SasA and CikA, which transduce this rhythm to control gene expression. Here, we describe crystal and nuclear magnetic resonance structures of KaiB-KaiC,KaiA-KaiB-KaiC, and CikA-KaiB complexes. They reveal how the metamorphic properties of KaiB, a protein that adopts two distinct folds, and the post-adenosine triphosphate hydrolysis state of KaiC create a hub around which nighttime signaling events revolve, including inactivation of KaiA and reciprocal regulation of the mutually antagonistic signaling proteins, SasA and CikA.

PubMed: 28302851
DOI: 10.1126/science.aag2516

実験手法

SOLUTION NMR