5JWQ

Crystal structure of KaiC S431E in complex with foldswitch-stabilized KaiB from Thermosynechococcus elongatus

5JWQ の概要

• エントリーDOI: 10.2210/pdb5jwq/pdb
• 関連するPDBエントリー: 5JWO 5JWR
• 分子名称: Circadian clock protein kinase KaiC, Circadian clock protein KaiB, ADENOSINE-5'-DIPHOSPHATE (3 entities in total)
• 機能のキーワード: transcription regulator, foldswitch
• 由来する生物種: Thermosynechococcus elongatus (strain BP-1); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 139822.10

構造登録者

Tseng, R.,Goularte, N.F.,Chavan, A.,Luu, J.,Chang, Y.,Heilser, J.,Tripathi, S.,LiWang, A.,Partch, C.L. (登録日: 2016-05-12, 公開日: 2017-03-29, 最終更新日: 2024-03-06)

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

X-RAY DIFFRACTION (3.871 Å)