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Structures of the cyanobacterial circadian oscillator frozen in a fully assembled state

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Schuller,  Jan M.
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Plitzko,  Jürgen M.
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Förster,  Friedrich
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Citation

Snijder, J., Schuller, J. M., Wiegard, A., Lossl, P., Schmelling, N., Axmann, I. M., et al. (2017). Structures of the cyanobacterial circadian oscillator frozen in a fully assembled state. Science, 355(6330), 1181-1184. doi:10.1126/science.aag3218.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002E-0A3F-B
Abstract
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 5'-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.