The influence of KaiA mutations on its function in the KaiABC circadian clock system

被引：1
|
作者：
Chen, Qiang [1 ]
Liu, Sen [1 ,2 ,3 ]
Yang, Liting [1 ]
Zhang, Lingya [1 ]
Li, Jinkui [1 ]
机构：
[1] China Three Gorges Univ, Med Coll, Hubei Key Lab Tumor Microenvironm & Immunotherapy, Yichang 443002, Peoples R China
[2] Hubei Univ Technol, Natl Ctr Cellular Regulat &Mol Pharmaceut 111, Wuhan 430068, Hubei, Peoples R China
[3] Hubei Univ Technol, Inst Biol & Pharmaceut Sci, Wuhan 430068, Hubei, Peoples R China
来源：
DATA IN BRIEF | 2018年 / 18卷
基金：
中国国家自然科学基金;
关键词：
KaiA; Circadian clock; Protein structure and function; Domain-swapping; Function switching;
D O I：
10.1016/j.dib.2018.03.032
中图分类号：
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
The core oscillator of the circadian clock of cyanobacteria consists of three proteins, KaiA, KaiB, and KaiC. The KaiABC oscillator can be re-constituted in vitro with the purified proteins in buffer containing ATP and Mg2+. The interaction between KaiA and KaiC has not been well studied. In this article, different KaiA mutants were designed and used to elucidate the influence of KaiA structure on its function in the in vitro system. Molecular dynamics simulations were adopted to study the structural flexibility of KaiA homodimer. The data presented in this article provide further experimental supports to our work in Chen et al. (2017) [1]. (C) 2018 The Authors. Published by Elsevier Inc.
引用
收藏
页码：241 / 247
页数：7
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