The “fishing a line” mechanism coupling ATP hydrolysis and KaiA-mediated up-regulation of autophosphorylation in the KaiC hexamer. The “fishing a line”

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The “fishing a line” mechanism coupling ATP hydrolysis and KaiA-mediated up-regulation of autophosphorylation in the KaiC hexamer. The “fishing a line” mechanism coupling ATP hydrolysis and KaiA-mediated up-regulation of autophosphorylation in the KaiC hexamer. (A) While both CI and CII domains harbor nucleotide-binding sites and ATPase-active sites at the subunit interfaces, the autokinase activity is exerted only in the CII domain. This is because the autophosphorylation sites (i.e., Ser431 and Thr432) are spatially proximal to the ATP molecule accommodated in the CII domain of the neighboring protomer. (B) In the CII AAA+ ring hexamer, ATP hydrolysis releases the A-loop, which thereby becomes reactive with KaiA. KaiA binding to the C-terminal segments of KaiC facilitates ADP release and ATP incorporation. The rapid ATP/ADP turnover leads to the up-regulation of autophosphorylation of KaiC. Yasuhiro Yunoki et al. LSA 2019;2:e201900368 © 2019 Yunoki et al.