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

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 (HK853^DHp), catalytic and ATP-binding domain (HK853^CA) and several linkers. HK853 can be completely autophosphorylated, which is the first step for signal transduction of TCS. HK853^CA is an essential domain for its kinase function, since HK853^CA could bind with ATP and convert it to ADP. Here, we report the backbone and part of side chain assignments of HK853^CA. By analyzing the chemical shifts of HN, N, CO, C^α and C^β, the secondary structure was predicted and contrasted with the published crystal structure of HK853^CA. The result showed that our predicted structure could basically fit into the crystal structure. Thus, the chemical shift assignments of HK853^CA are the starting point for further structural and dynamics study.