ArticleActa crystallographica. Section D, Biological crystallography2014
An arginine tetrad as mediator of input-dependent and input-independent ATPases in the clock protein KaiC.
Article in Acta crystallographica. Section D, Biological crystallography, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 20 citations in OpenAlex.
- The cyanobacterial circadian clock.Npj biological timing and sleep · 2025Review
- The inner workings of an ancient biological clock.Trends in biochemical sciences · 2024Review
- Coupling of distant ATPase domains in the circadian clock protein KaiC.Nature structural & molecular biology · 2022Article
- Regulation mechanisms of the dual ATPase in KaiC.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Elucidation of master allostery essential for circadian clock oscillation in cyanobacteria.Science advances · 2022Article
- ATP hydrolysis by KaiC promotes its KaiA binding in the cyanobacterial circadian clock system.Life science alliance · 2019Article
- Molecular dynamics simulations of nucleotide release from the circadian clock protein KaiC reveal atomic-resolution functional insights.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Minimal tool set for a prokaryotic circadian clock.BMC evolutionary biology · 2017Article
- Architecture and mechanism of the central gear in an ancient molecular timer.Journal of the Royal Society, Interface · 2017Review
- Intricate protein-protein interactions in the cyanobacterial circadian clock.The Journal of biological chemistry · 2014Review
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
A post-translational oscillator (PTO) composed of the proteins KaiA, KaiB and KaiC is at the heart of the cyanobacterial circadian clock. KaiC interacts with KaiA and KaiB over the daily cycle, and CII domains undergo rhythmic phosphorylation/dephosphorylation with a 24 h period. Both the N-terminal (CI) and C-terminal (CII) rings of KaiC exhibit ATPase activity. The CI ATPase proceeds in an input-independent fashion, but the CII ATPase is subject to metabolic input signals. The crystal structure of KaiC from Thermosynechococcus elongatus allows insight into the different anatomies of the CI and CII ATPases. Four consecutive arginines in CI (Arg linker) that connect the P-loop, CI subunits and CI and CII at the ring interface are primary candidates for the coordination of the CI and CII activities. The mutation of linker residues alters the period or triggers arhythmic behavior. Comparison between the CI and CII structures also reveals differences in loop regions that are key to KaiA and KaiB binding and activation of CII ATPase and kinase. Common packing features in KaiC crystals shed light on the KaiB-KaiC interaction.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.