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Villarreal, Seth A. Here, we present a crystallographic structure of the wild-type Synechococcus elongatus KaiB and a cryo-electron microscopy cryoEM structure of a KaiBC complex. The crystal structure shows the expected dimer core structure and significant conformational variations of the KaiB Tooleping aktsiaoptsioonidega region, which is functionally important in maintaining Bollinger Stripi uuring.

A KaiC mutation, RC, which has been shown to affect the affinity of KaiB for KaiC and lengthen the period in a bioluminescence rhythm assay, is found within the middle of the predicted KaiBC interface.

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We demonstrate here that the AV KaiC mutant sheds light on the former mechanism. It was previously reported that AV is less sensitive to dark pulse-induced phase resetting and has a reduced amplitude of the KaiC phosphorylation rhythm in vivo.

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A maps to a loop loop that continues toward the phosphorylation sites. By pulling on the C-terminal peptide of KaiC A-loopKaiA removes restraints from the adjacent loop whose increased flexibility indirectly promotes kinase activity. We found in the crystal structure that AV KaiC lacks phosphorylation at S and exhibits a subtle, local conformational change relative to wild-type KaiC.

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Molecular dynamics simulations indicate higher mobility of the loop in the absence of the A-loop and mobility differences in other areas associated with phosphorylation activity between wild-type and mutant KaiCs. Finally, the A-loop—loop Bollinger Stripi uuring that informs KaiC phosphorylation sites of KaiA dimer binding propagates to loops from neighboring KaiC subunits, thus providing support for a concerted allosteric mechanism of phosphorylation.

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