Chemical shift assignments of the catalytic and ATP-binding domain of HK853 from Thermotoga maritime

  • Yuan Zhou
  • Xinghong Liu
  • Conggang Li
  • Maili Liu
  • Ling Jiang
  • Yixiang LiuEmail author


HK853 is a transmembrane protein from Thermotoga maritime, which belongs to HK853/RR468 two-component signal transduction system (TCS) and acts as a sensor histidine kinase. HK853 is mainly composed of a transmembrane domain, dimerization and histidine-containing phosphotransfer domain (HK853DHp), catalytic and ATP-binding domain (HK853CA) and several linkers. HK853 can be completely autophosphorylated, which is the first step for signal transduction of TCS. HK853CA is an essential domain for its kinase function, since HK853CA could bind with ATP and convert it to ADP. Here, we report the backbone and part of side chain assignments of HK853CA. By analyzing the chemical shifts of HN, N, CO, Cα and Cβ, the secondary structure was predicted and contrasted with the published crystal structure of HK853CA. The result showed that our predicted structure could basically fit into the crystal structure. Thus, the chemical shift assignments of HK853CA are the starting point for further structural and dynamics study.


Chemical shift assignment NMR HK853CA Secondary structure HSQC 



This project was supported by Grants from National Key R&D Program of China (#2017YFA0505400) and the Natural Science Foundation of China (#21573280 and #21603268).

Compliance with ethical standards

Conflict of interest

The authors declare that they have no conflict of interest.


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© Springer Nature B.V. 2019

Authors and Affiliations

  1. 1.Key Laboratory of Magnetic Resonance in Biological Systems, National Center for Magnetic Resonance in Wuhan, State Key Laboratory of Magnetic Resonance and Atomic and Molecular PhysicsWuhan Institute of Physics and Mathematics, The Chinese Academy of SciencesWuhanChina
  2. 2.Graduate University of Chinese Academy of ScienceBeijingChina

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