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. 2018 May 26;15:136–150. doi: 10.2142/biophysico.15.0_136

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2018 © The Biophysical Society of Japan

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Coarse-grained models of the KaiABC system. a) Schematic of interactions among Kai proteins considered in the MM model. Two phosphorylation sites, Ser431 and Thr432, of each subunit in the CII domain (blue) are repeatedly phosphorylated (pS, pT) and dephosphorylated (S, T). KaiA dimer (red) binds to KaiC hexamer C₆ to form C₆A₂. The CI (pink) of each subunit binds to KaiB (cyan) to form C₆B_i with 1 ≤ i ≤ 6, which further binds to KaiA dimers to form C₆B_iA₂_j with 1 ≤ j ≤ i. b) Reactions and states in a KaiC subunit in the SM model. ATP hydrolysis reactions and KaiB binding/dissociation reactions occur in the CI domain (pink). Phosphorylation (P)/dephosphorylation (dP) reactions and KaiA binding/dissociation reactions take place in the CII domain (blue). CI and CII domains are coupled through allosteric structural change.