Structural Studies on Auto-regulatory Mechanism of Cyanobacterial Clock Proteins

点击翻译按钮获取中文摘要

Dynamic structural change of the KaiC hexamer revealed in this study provides notable insights into the cyanobacterial circadian clock. Our model implies that KaiC ticks through expanding and contracting motions of the C2 ring. The timing of the accumulation of KaiC carrying the expanded C2 ring is coincident with that of accumulation of KaiC associated both with KaiA and KaiB. The conformational ticking of KaiC is likely to serve as a timing cue for assembly/disassembly of KaiA and KaiB.