2022
DOI: 10.1038/s41594-022-00803-w
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Coupling of distant ATPase domains in the circadian clock protein KaiC

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Cited by 9 publications
(14 citation statements)
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“…A recently solved cryo-EM structure of the night-time phosphomimetic KaiC SE -S431E/T432A in its compressed state directly showed a disordered A loop that no longer interacts with the 422 loop 19 , similar to the extended A loop conformation we observed in KaiC RS (Fig. 1e).…”
Section: A Coiled-coil Interaction Assembles a Kaic Rs Dodecamersupporting
confidence: 68%
See 3 more Smart Citations
“…A recently solved cryo-EM structure of the night-time phosphomimetic KaiC SE -S431E/T432A in its compressed state directly showed a disordered A loop that no longer interacts with the 422 loop 19 , similar to the extended A loop conformation we observed in KaiC RS (Fig. 1e).…”
Section: A Coiled-coil Interaction Assembles a Kaic Rs Dodecamersupporting
confidence: 68%
“…This hypothesis was based on the perceived hyperphosphorylation and hypophosphorylation that occurred after removing the A loop or disrupting KaiA binding, respectively 18 . A recently solved cryo-EM structure of the night-time phosphomimetic KaiC SE -S431E/T432A in its compressed state directly showed a disordered A loop that no longer interacts with the 422 loop 19 , similar to the extended A loop conformation we observed in KaiC RS (Fig. 1e ).…”
Section: A Coiled-coil Interaction Assembles a Kaic Rs ...supporting
confidence: 68%
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“…Recent cryo‐EM studies on KaiC phosphomimetics support this model. [ 52,53 ] The phosphorylation‐dependent CII ring dynamics promotes clockwise movement through this phosphorylation cycle and prevents counterclockwise phosphorylation activity. [ 27 ] The decrease in KaiA–KaiC affinity as the A‐loops become progressively sequestered with increasing levels of phosphorylated S431 also provides an explanation for the maintenance of phase coherence across an ensemble of clock proteins.…”
Section: Introductionmentioning
confidence: 99%