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TitleStructures of the cyanobacterial circadian oscillator frozen in a fully assembled state.
Journal, issue, pagesScience, Vol. 355, Issue 6330, Page 1181-1184, Year 2017
Publish dateMar 17, 2017
AuthorsJoost Snijder / Jan M Schuller / Anika Wiegard / Philip Lössl / Nicolas Schmelling / Ilka M Axmann / Jürgen M Plitzko / Friedrich Förster / Albert J R Heck /
PubMed AbstractCyanobacteria 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 ...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.
External linksScience / PubMed:28302852
MethodsEM (single particle)
Resolution4.7 - 7.0 Å
Structure data

3602

5n8y

EMDB-3602, PDB-5n8y:
KaiCBA circadian clock backbone model based on a Cryo-EM density
Method: EM (single particle) / Resolution: 4.7 Å

EMDB-3603:
KaiCB circadian clock backbone model based on a Cryo-EM density
Method: EM (single particle) / Resolution: 7.0 Å

Source
  • synechococcus elongatus (bacteria)
KeywordsTRANSFERASE / AAA+-ATPase / Kinase / Circadian Clock Complex / Cyanobacteria / Fold-switch

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