S.-i. Koda

This study investigates how the dual ATPase activities in KaiC coordinate to regulate the cyanobacterial circadian clock through structural and biochemical analysis.

This paper investigates how the ring-shaped hexameric structure of KaiC enables acceleration of KaiB-KaiC complex formation through cooperative binding, despite ADP/ATP exchange inhibition typically slowing processes.

This study proposes a new binding mechanism for KaiB-KaiC in cyanobacteria that explains the slowness of the circadian rhythm without requiring conformational changes in KaiB.

This study shows that unidirectional allostery from C2 to C1 in KaiC is sufficient to generate the cyanobacterial circadian rhythm, as demonstrated by matching experimental data on phosphorylation and ATPase activity.