ArticleJournal of molecular biology2013
CryoEM and molecular dynamics of the circadian KaiB-KaiC complex indicates that KaiB monomers interact with KaiC and block ATP binding clefts.
Article in Journal of molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- Programming scheduled self-assembly of circadian materials.Nature communications · 2025Article
- Article
- Dimer dissociation is a key energetic event in the fold-switch pathway of KaiB.Biophysical journal · 2022Article
- Monitoring Protein-Protein Interactions in the Cyanobacterial Circadian Clock in Real Time via Electron Paramagnetic Resonance Spectroscopy.Biochemistry · 2020Article
- Orchestration of Circadian Timing by Macromolecular Protein Assemblies.Journal of molecular biology · 2020Review
- Article
- Less Is More: Coarse-Grained Integrative Modeling of Large Biomolecular Assemblies with HADDOCK.Journal of chemical theory and computation · 2019Article
- Minimal tool set for a prokaryotic circadian clock.BMC evolutionary biology · 2017Article
- Structural basis of the day-night transition in a bacterial circadian clock.Science (New York, N.Y.) · 2017Article
- Architecture and mechanism of the central gear in an ancient molecular timer.Journal of the Royal Society, Interface · 2017Review
- A thermodynamically consistent model of the post-translational Kai circadian clock.PLoS computational biology · 2017Article
- Structural characterization of the circadian clock protein complex composed of KaiB and KaiC by inverse contrast-matching small-angle neutron scattering.Scientific reports · 2016Article
- A dynamic interaction process between KaiA and KaiC is critical to the cyanobacterial circadian oscillator.Scientific reports · 2016Article
- Circadian Clocks: Unexpected Biochemical Cogs.Current biology : CB · 2015Article
- Circadian rhythms. A protein fold switch joins the circadian oscillator to clock output in cyanobacteria.Science (New York, N.Y.) · 2015Article
- Detecting KaiC phosphorylation rhythms of the cyanobacterial circadian oscillator in vitro and in vivo.Methods in enzymology · 2015Article
- Mixtures of opposing phosphorylations within hexamers precisely time feedback in the cyanobacterial circadian clock.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Intricate protein-protein interactions in the cyanobacterial circadian clock.The Journal of biological chemistry · 2014Review
- An arginine tetrad as mediator of input-dependent and input-independent ATPases in the clock protein KaiC.Acta crystallographica. Section D, Biological crystallography · 2014Article
- Exchange of ADP with ATP in the CII ATPase domain promotes autophosphorylation of cyanobacterial clock protein KaiC.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
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Authors and funding
8 authors.
Funding
Abstract
The circadian control of cellular processes in cyanobacteria is regulated by a posttranslational oscillator formed by three Kai proteins. During the oscillator cycle, KaiA serves to promote autophosphorylation of KaiC while KaiB counteracts this effect. Here, we present a crystallographic structure of the wild-type Synechococcus elongatus KaiB and a cryo-electron microscopy (cryoEM) structure of a KaiBC complex. The crystal structure shows the expected dimer core structure and significant conformational variations of the KaiB C-terminal region, which is functionally important in maintaining rhythmicity. The KaiBC sample was formed with a C-terminally truncated form of KaiC, KaiC-Δ489, which is persistently phosphorylated. The KaiB-KaiC-Δ489 structure reveals that the KaiC hexamer can bind six monomers of KaiB, which form a continuous ring of density in the KaiBC complex. We performed cryoEM-guided molecular dynamics flexible fitting simulations with crystal structures of KaiB and KaiC to probe the KaiBC protein-protein interface. This analysis indicated a favorable binding mode for the KaiB monomer on the CII end of KaiC, involving two adjacent KaiC subunits and spanning an ATP binding cleft. A KaiC mutation, R468C, which has been shown to affect the affinity of KaiB for KaiC and lengthen the period in a bioluminescence rhythm assay, is found within the middle of the predicted KaiBC interface. The proposed KaiB binding mode blocks access to the ATP binding cleft in the CII ring of KaiC, which provides insight into how KaiB might influence the phosphorylation status of KaiC.
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