5N8Y
KaiCBA circadian clock backbone model based on a Cryo-EM density
Summary for 5N8Y
Entry DOI | 10.2210/pdb5n8y/pdb |
EMDB information | 3602 |
Descriptor | Circadian clock protein kinase KaiC, Circadian clock protein KaiB, Circadian clock protein KaiA (3 entities in total) |
Functional Keywords | aaa+-atpase, kinase, circadian clock complex, cyanobacteria, fold-switch, transferase |
Biological source | Synechococcus elongatus More |
Total number of polymer chains | 24 |
Total formula weight | 809133.35 |
Authors | Schuller, J.M.,Snijder, J.,Loessl, P.,Heck, A.J.R.,Foerster, F. (deposition date: 2017-02-24, release date: 2017-03-29, Last modification date: 2024-05-15) |
Primary citation | Snijder, J.,Schuller, J.M.,Wiegard, A.,Lossl, P.,Schmelling, N.,Axmann, I.M.,Plitzko, J.M.,Forster, F.,Heck, A.J. Structures of the cyanobacterial circadian oscillator frozen in a fully assembled state. Science, 355:1181-1184, 2017 Cited by PubMed 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. PubMed: 28302852DOI: 10.1126/science.aag3218 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (4.7 Å) |
Structure validation
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