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Snijder, Joost; Schuller, Jan M.; Wiegard, Anika; Lössl, Philip; Schmelling, Nicolas; Axmann, Ilka M.; Plitzko, Jürgen M.; Förster, Friedrich; Heck, Albert J. R.
Science (American Association for the Advancement of Science), 03/2017, Volume: 355, Issue: 6330Journal Article
Cyanobacteria have a robust circadian oscillator, known as the Kai system. Reconstituted from the purified protein components KaiC, KaiB, and KaiA, it can tick autonomously in the presence of adenosine 5ʹ-triphosphate (ATP). The KaiC hexamers enter a natural 24-hour reaction cycle of autophosphorylation and assembly with KaiB and KaiA in numerous diverse forms. We describe the preparation of stoichiometrically well-defined assemblies of KaiCB and KaiCBA, as monitored by native mass spectrometry, allowing for a structural characterization by single-particle cryo–electron microscopy and mass spectrometry. Our data reveal details of the interactions between the Kai proteins and provide a structural basis to understand periodic assembly of the protein oscillator.
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