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

Snijder, Joost; Schuller, Jan M.; Wiegard, Anika; Lossl, Philip; Schmelling, Nicolas; Axmann, Ilka M.; Plitzko, Jürgen M.; Förster, Friedrich; Heck, Albert J. R.

doi:10.1126/science.aag3218

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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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引用

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

引用: https://hdl.handle.net/11858/00-001M-0000-002E-0A3F-B

要旨

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.