An arginine tetrad as mediator of input-dependent and input-independent ATPases in the clock protein KaiC.

An arginine tetrad as mediator of input-dependent and input-independent ATPases in the clock protein KaiC.
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精氨酸四联体作为时钟蛋白 KaiC 中输入依赖性和输入非依赖性 ATP 酶的介体。

DOI:
10.1107/s1399004714003228
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发表时间:
2014
期刊:
Acta crystallographica. Section D, Biological crystallography
影响因子:
--
通讯作者:
Egli,Martin
Egli,Martin
中科院分区:
--
文献类型:
--
作者:
Pattanayek,Rekha;Xu,Yao;Lamichhane,Aashish;Johnson,CarlH;Egli,Martin

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由蛋白KaiA、KaiB和KaiC组成的翻译后振荡器(PTO)是蓝藻生物钟的核心。KaiC与KaiA和KaiB在每天的周期内相互作用,并且CII结构域以24小时为周期进行有节奏的磷酸化/去磷酸化。KaiC的n端(CI)和c端(CII)环均表现出atp酶活性。CI atp酶以独立于输入的方式进行,但CII atp酶受代谢输入信号的影响。从长热聚球菌中提取的KaiC的晶体结构可以深入了解CI和CII atp酶的不同解剖结构。在环界面上连接p环、CI亚基以及CI和CII的四个连续精氨酸(Arg linker)是协调CI和CII活性的主要候选者。连接体残基的突变改变周期或触发节律性行为。CI和CII结构的比较也揭示了环区的差异,环区是KaiA和KaiB结合以及CII atp酶和激酶激活的关键。KaiC晶体中常见的填充特征揭示了KaiB-KaiC相互作用。
A post-translational oscillator (PTO) composed of the proteins KaiA, KaiB and KaiC is at the heart of the cyanobacterial circadian clock. KaiC interacts with KaiA and KaiB over the daily cycle, and CII domains undergo rhythmic phosphorylation/dephosphorylation with a 24 h period. Both the N-terminal (CI) and C-terminal (CII) rings of KaiC exhibit ATPase activity. The CI ATPase proceeds in an input-independent fashion, but the CII ATPase is subject to metabolic input signals. The crystal structure of KaiC from Thermosynechococcus elongatus allows insight into the different anatomies of the CI and CII ATPases. Four consecutive arginines in CI (Arg linker) that connect the P-loop, CI subunits and CI and CII at the ring interface are primary candidates for the coordination of the CI and CII activities. The mutation of linker residues alters the period or triggers arhythmic behavior. Comparison between the CI and CII structures also reveals differences in loop regions that are key to KaiA and KaiB binding and activation of CII ATPase and kinase. Common packing features in KaiC crystals shed light on the KaiB–KaiC interaction.
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