4TLC

Crystal structure of N-terminal C1 domain of KaiC

4TLC の概要

• エントリーDOI: 10.2210/pdb4tlc/pdb
• 関連するPDBエントリー: 4TL6 4TL7 4TL8 4TL9 4TLA 4TLB 4TLD 4TLE
• 分子名称: Circadian clock protein kinase KaiC, MAGNESIUM ION, CHLORIDE ION, ... (5 entities in total)
• 機能のキーワード: serine/threonine-protein kinase, transferase
• 由来する生物種: Synechococcus elongatus PCC 7942
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 173593.10

構造登録者

Abe, J.,Hiyama, T.B.,Mukaiyama, A.,Son, S.,Akiyama, S. (登録日: 2014-05-29, 公開日: 2015-07-01, 最終更新日: 2024-03-20)

主引用文献

Abe, J.,Hiyama, T.B.,Mukaiyama, A.,Son, S.,Mori, T.,Saito, S.,Osako, M.,Wolanin, J.,Yamashita, E.,Kondo, T.,Akiyama, S.
Atomic-scale origins of slowness in the cyanobacterial circadian clock
Science, 349:312-316, 2015

PubMed Abstract: Circadian clocks generate slow and ordered cellular dynamics but consist of fast-moving bio-macromolecules; consequently, the origins of the overall slowness remain unclear. We identified the adenosine triphosphate (ATP) catalytic region [adenosine triphosphatase (ATPase)] in the amino-terminal half of the clock protein KaiC as the minimal pacemaker that controls the in vivo frequency of the cyanobacterial clock. Crystal structures of the ATPase revealed that the slowness of this ATPase arises from sequestration of a lytic water molecule in an unfavorable position and coupling of ATP hydrolysis to a peptide isomerization with high activation energy. The slow ATPase is coupled with another ATPase catalyzing autodephosphorylation in the carboxyl-terminal half of KaiC, yielding the circadian response frequency of intermolecular interactions with other clock-related proteins that influences the transcription and translation cycle.

PubMed: 26113637
DOI: 10.1126/science.1261040

実験手法

X-RAY DIFFRACTION (2.09 Å)