7DY2

Crystal Structure of Cyanobacterial Circadian Clock Protein KaiC

7DY2 の概要

• エントリーDOI: 10.2210/pdb7dy2/pdb
• 関連するPDBエントリー: 7DXQ
• 分子名称: Circadian clock protein kinase KaiC, ADENOSINE-5'-DIPHOSPHATE, ADENOSINE-5'-TRIPHOSPHATE, ... (6 entities in total)
• 機能のキーワード: clock protein, transferase
• 由来する生物種: Synechococcus elongatus (strain PCC 7942 / FACHB-805); 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 709337.25

構造登録者

Furuike, Y.,Akiyama, S. (登録日: 2021-01-20, 公開日: 2022-04-27, 最終更新日: 2024-11-20)

主引用文献

Furuike, Y.,Mukaiyama, A.,Ouyang, D.,Ito-Miwa, K.,Simon, D.,Yamashita, E.,Kondo, T.,Akiyama, S.
Elucidation of master allostery essential for circadian clock oscillation in cyanobacteria.
Sci Adv, 8:eabm8990-eabm8990, 2022

PubMed Abstract: Spatiotemporal allostery is the source of complex but ordered biological phenomena. To identify the structural basis for allostery that drives the cyanobacterial circadian clock, we crystallized the clock protein KaiC in four distinct states, which cover a whole cycle of phosphor-transfer events at Ser and Thr. The minimal set of allosteric events required for oscillatory nature is a bidirectional coupling between the coil-to-helix transition of the Ser-dependent phospho-switch in the C-terminal domain of KaiC and adenosine 5'-diphosphate release from its N-terminal domain during adenosine triphosphatase cycle. An engineered KaiC protein oscillator consisting of a minimal set of the identified master allosteric events exhibited a monophosphorylation cycle of Ser with a temperature-compensated circadian period, providing design principles for simple posttranslational biochemical circadian oscillators.

PubMed: 35427168
DOI: 10.1126/sciadv.abm8990

実験手法

X-RAY DIFFRACTION (3.04 Å)