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

Qiang Chen; Sen Liu; Liting Yang; Lingya Zhang; Jinkui Li

doi:10.1016/j.dib.2018.03.032

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

Data Brief. 2018 Mar 12:18:241-247. doi: 10.1016/j.dib.2018.03.032. eCollection 2018 Jun.

Authors

Qiang Chen¹, Sen Liu^{1

2}, Liting Yang¹, Lingya Zhang¹, Jinkui Li¹

Affiliations

¹ Hubei Key Laboratory of Tumor Microenvironment and Immunotherapy, Medical College, China Three Gorges University, Yichang 443002, China.
² National "111" Center for Cellular Regulation and Molecular Pharmaceutics & Institute of Biomedical and Pharmaceutical Sciences, Hubei University of Technology, Wuhan 430068, China.

Abstract

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].

Keywords: Circadian clock; Domain-swapping; Function switching; KaiA; Protein structure and function.