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7DY2

Crystal Structure of Cyanobacterial Circadian Clock Protein KaiC

Summary for 7DY2
Entry DOI10.2210/pdb7dy2/pdb
Related7DXQ
DescriptorCircadian clock protein kinase KaiC, ADENOSINE-5'-DIPHOSPHATE, ADENOSINE-5'-TRIPHOSPHATE, ... (6 entities in total)
Functional Keywordsclock protein, transferase
Biological sourceSynechococcus elongatus (strain PCC 7942 / FACHB-805)
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Total number of polymer chains12
Total formula weight709337.25
Authors
Furuike, Y.,Akiyama, S. (deposition date: 2021-01-20, release date: 2022-04-27, Last modification date: 2024-11-20)
Primary citationFuruike, Y.,Mukaiyama, A.,Ouyang, D.,Ito-Miwa, K.,Simon, D.,Yamashita, E.,Kondo, T.,Akiyama, S.
Elucidation of master allostery essential for circadian clock oscillation in cyanobacteria.
Sci Adv, 8:eabm8990-eabm8990, 2022
Cited by
PubMed Abstract: Spatiotemporal 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 and Thr. The minimal set of allosteric events required for oscillatory nature is a bidirectional coupling between the coil-to-helix transition of the Ser-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 with a temperature-compensated circadian period, providing design principles for simple posttranslational biochemical circadian oscillators.
PubMed: 35427168
DOI: 10.1126/sciadv.abm8990
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.04 Å)
Structure validation

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