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Structural highlights

Function

KAIA_THEVB Key component of the KaiABC oscillator complex, which constitutes the main circadian regulator in cyanobacteria. Complex composition changes during the circadian cycle to control KaiC phosphorylation. KaiA stimulates KaiC autophosphorylation, while KaiB sequesters KaiA, leading to KaiC autodephosphorylation. KaiA binding to the KaiC CII domain during the subjective day yields KaiA(2-4):KaiC(6) complexes which stimulate KaiC autophosphorylation. Phospho-Ser-431 KaiC accumulation triggers binding of KaiB during the subjective night to form the KaiB(6):KaiC(6) complex, leading to changes in the output regulators CikA and SasA. KaiB(6):KaiC(6) formation exposes a site for KaiA binding on KaiB that sequesters KaiA from KaiC's CII domain, making the KaiC(6):KaiB(6):KaiA(12) complex resulting in KaiC autodephosphorylation. Complete dephosphorylation of KaiC leads to dissociation of KaiA(2):KaiB(1), completing 1 cycle of the Kai oscillator (By similarity). Formation of the KaiB:KaiC complex is promoted by KaiA, helping switch KaiC from its autophosphorylation to autodephosphatase function (PubMed:24112939).[UniProtKB:Q79PF6]^[1] Binds oxidized quinones via the N-terminal PsR domain, allowing it to sense redox changes and possibly mediate clock input.[UniProtKB:Q79PF6]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

• Circadian clock protein 3D structures

References

1. ↑ Tseng R, Chang YG, Bravo I, Latham R, Chaudhary A, Kuo NW, Liwang A. Cooperative KaiA-KaiB-KaiC interactions affect KaiB/SasA competition in the circadian clock of cyanobacteria. J Mol Biol. 2014 Jan 23;426(2):389-402. PMID:24112939 doi:10.1016/j.jmb.2013.09.040