7dyk
Crystal Structure of Cyanobacterial Circadian Clock Protein KaiC
Structural highlights
FunctionKAIC_SYNE7 Core component of the KaiABC clock protein complex, which constitutes the main circadian regulator in cyanobacteria. Binds to DNA. The KaiABC complex may act as a promoter-nonspecific transcription regulator that represses transcription, possibly by acting on the state of chromosome compaction.[1] [2] Publication Abstract from PubMedSpatiotemporal allostery is the source of complex but ordered biological phenomena. To identify the structural basis for allostery that drives the cyanobacterial circadian clock, we crystallized the clock protein KaiC in four distinct states, which cover a whole cycle of phosphor-transfer events at Ser(431) and Thr(432). The minimal set of allosteric events required for oscillatory nature is a bidirectional coupling between the coil-to-helix transition of the Ser(431)-dependent phospho-switch in the C-terminal domain of KaiC and adenosine 5'-diphosphate release from its N-terminal domain during adenosine triphosphatase cycle. An engineered KaiC protein oscillator consisting of a minimal set of the identified master allosteric events exhibited a monophosphorylation cycle of Ser(431) with a temperature-compensated circadian period, providing design principles for simple posttranslational biochemical circadian oscillators. Elucidation of master allostery essential for circadian clock oscillation in cyanobacteria.,Furuike Y, Mukaiyama A, Ouyang D, Ito-Miwa K, Simon D, Yamashita E, Kondo T, Akiyama S Sci Adv. 2022 Apr 15;8(15):eabm8990. doi: 10.1126/sciadv.abm8990. Epub 2022 Apr, 15. PMID:35427168[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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