Chemical shift assignments of the catalytic and ATP-binding domain of HK853 from Thermotoga maritime
Chemical shift assignments of the catalytic and ATP-binding domain of HK853 from Thermotoga maritime
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来自 Thermotoga Maritime 的 HK853 的催化和 ATP 结合结构域的化学位移分配
DOI：
10.1007/s12104-019-09872-3
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发表时间：
2019
影响因子：
0.9
通讯作者：
Liu Yixiang
中科院分区：
文献类型：
--
作者：
Zhou Yuan;Liu Xinghong;Li Conggang;Liu Maili;Jiang Ling;Liu Yixiang
HK 853是海栖热袍菌（Thermotoga maritime）的一种跨膜蛋白，属于HK 853/RR 468双组分信号转导系统（TCS），是一种感受组氨酸激酶。HK 853主要由一个跨膜结构域、二聚化和含组氨酸的磷酸转移结构域（HK 853 DHp）、催化和ATP结合结构域（HK 853 CA）和几个接头组成。HK 853可以完全自磷酸化，这是TCS信号转导的第一步。HK 853 CA是其激酶功能的必需结构域，因为HK 853 CA可以与ATP结合并将其转化为ADP。在这里，我们报告的骨干和部分侧链分配的HK 853 CA。通过分析HN、N、CO、Cα和Cβ的化学位移，预测了HK 853 CA的二级结构，并与已发表的HK 853 CA晶体结构进行了对比。结果表明，我们预测的结构与晶体结构基本吻合。因此，HK 853 CA的化学位移归属是进一步结构和动力学研究的起点。
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.