Chemical shift assignments of the catalytic and ATP-binding domain of HK853 from Thermotoga maritime
文献类型：期刊论文
| 作者 | Liu, Yixiang2; Jiang, Ling2; Liu, Maili2; Li, Conggang2; Liu, Xinghong1,2; Zhou, Yuan1,2 |
| 刊名 | BIOMOLECULAR NMR ASSIGNMENTS
 |
| 出版日期 | 2019-04-01 |
| 卷号 | 13期号:1页码:173-176 |
| ISSN号 | 1874-2718 |
| 关键词 | Chemical shift assignment NMR HK853(CA) Secondary structure HSQC |
| 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. |
| WOS关键词 | BACTERIAL HISTIDINE KINASES ; PHOSPHATASE-ACTIVITY ; SIGNAL-TRANSDUCTION ; 2-COMPONENT |
| 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 |
| 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. |
入库方式： OAI收割
来源：武汉物理与数学研究所
浏览0
下载0
收藏0
其他版本
除非特别说明，本系统中所有内容都受版权保护，并保留所有权利。