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

doi:10.1007/s12104-019-09872-3

	Chemical shift assignments of the catalytic and ATP-binding domain of HK853 from Thermotoga maritime
	Liu, Yixiang 2; Jiang, Ling 2; Liu, Maili 2; Li, Conggang 2; Liu, Xinghong 1,2; Zhou, Yuan 1,2
刊名	BIOMOLECULAR NMR ASSIGNMENTS
	2019-04-01
卷号	13 期号:1 页码:173-176
关键词	Chemical shift assignment NMR HK853(CA) Secondary structure HSQC
ISSN号	1874-2718
DOI	10.1007/s12104-019-09872-3
英文摘要	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 and C, 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.
资助项目	National Key R&D Program of China[2017YFA0505400] ; Natural Science Foundation of China[21573280] ; Natural Science Foundation of China[21603268]
WOS关键词	BACTERIAL HISTIDINE KINASES ; PHOSPHATASE-ACTIVITY ; SIGNAL-TRANSDUCTION ; 2-COMPONENT
WOS研究方向	Biophysics ; Spectroscopy
语种	英语
出版者	SPRINGER
WOS记录号	WOS:000463649500033
资助机构	National Key R&D Program of China ; National Key R&D Program of China ; Natural Science Foundation of China ; Natural Science Foundation of China ; National Key R&D Program of China ; National Key R&D Program of China ; Natural Science Foundation of China ; Natural Science Foundation of China ; National Key R&D Program of China ; National Key R&D Program of China ; Natural Science Foundation of China ; Natural Science Foundation of China ; National Key R&D Program of China ; National Key R&D Program of China ; Natural Science Foundation of China ; Natural Science Foundation of China
内容类型	期刊论文
源URL	[http://ir.wipm.ac.cn/handle/112942/13743]
专题	中国科学院武汉物理与数学研究所
通讯作者	Liu, Yixiang
作者单位	1.Chinese Acad Sci, Grad Univ, Beijing 100049, Peoples R China 2.Chinese Acad Sci, State Key Lab Magnet Resonance & Atom & Mol Phys, Key Lab Magnet Resonance Biol Syst, Natl Ctr Magnet Resonance Wuhan,Wuhan Inst Phys &, Wuhan 430071, Hubei, Peoples R China
推荐引用方式 GB/T 7714	Liu, Yixiang,Jiang, Ling,Liu, Maili,et al. Chemical shift assignments of the catalytic and ATP-binding domain of HK853 from Thermotoga maritime[J]. BIOMOLECULAR NMR ASSIGNMENTS,2019,13(1):173-176.
APA	Liu, Yixiang,Jiang, Ling,Liu, Maili,Li, Conggang,Liu, Xinghong,&Zhou, Yuan.(2019).Chemical shift assignments of the catalytic and ATP-binding domain of HK853 from Thermotoga maritime.BIOMOLECULAR NMR ASSIGNMENTS,13(1),173-176.
MLA	Liu, Yixiang,et al."Chemical shift assignments of the catalytic and ATP-binding domain of HK853 from Thermotoga maritime".BIOMOLECULAR NMR ASSIGNMENTS 13.1(2019):173-176.