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-Structure paper
タイトル | Coupling of distant ATPase domains in the circadian clock protein KaiC. |
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ジャーナル・号・ページ | Nat Struct Mol Biol, Vol. 29, Issue 8, Page 759-766, Year 2022 |
掲載日 | 2022年7月21日 |
著者 | Jeffrey A Swan / Colby R Sandate / Archana G Chavan / Alfred M Freeberg / Diana Etwaru / Dustin C Ernst / Joseph G Palacios / Susan S Golden / Andy LiWang / Gabriel C Lander / Carrie L Partch / |
PubMed 要旨 | The AAA family member KaiC is the central pacemaker for circadian rhythms in the cyanobacterium Synechococcus elongatus. Composed of two hexameric rings of adenosine triphosphatase (ATPase) domains ...The AAA family member KaiC is the central pacemaker for circadian rhythms in the cyanobacterium Synechococcus elongatus. Composed of two hexameric rings of adenosine triphosphatase (ATPase) domains with tightly coupled activities, KaiC undergoes a cycle of autophosphorylation and autodephosphorylation on its C-terminal (CII) domain that restricts binding of clock proteins on its N-terminal (CI) domain to the evening. Here, we use cryogenic-electron microscopy to investigate how daytime and nighttime states of CII regulate KaiB binding on CI. We find that the CII hexamer is destabilized during the day but takes on a rigidified C-symmetric state at night, concomitant with ring-ring compression. Residues at the CI-CII interface are required for phospho-dependent KaiB association, coupling ATPase activity on CI to cooperative KaiB recruitment. Together, these studies clarify a key step in the regulation of cyanobacterial circadian rhythms by KaiC phosphorylation. |
リンク | Nat Struct Mol Biol / PubMed:35864165 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 2.8 - 3.8 Å |
構造データ | EMDB-24850, PDB-7s65: EMDB-24851, PDB-7s66: EMDB-24852, PDB-7s67: |
化合物 | ChemComp-MG: ChemComp-ADP: ChemComp-ATP: |
由来 |
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キーワード | CIRCADIAN CLOCK PROTEIN / AAA ATPase / Circadian Oscillator / Kinase / Phosphatase |