Backbone resonance assignment of the response regulator protein PhoB(N) (F20D) from Escherichia coli
文献类型：期刊论文
| 作者 | Kou, Xinhui1,2; Liu, Xinghong1,2; Liu, Yixiang2; Li, Conggang2; Liu, Maili2; Jiang, Ling2 |
| 刊名 | BIOMOLECULAR NMR ASSIGNMENTS
 |
| 出版日期 | 2018-04-01 |
| 卷号 | 12期号:1页码:133-137 |
| 关键词 | Chemical Shift Assignment Nmr Phob(n)(F20d) Secondary Structure Hsqc |
| ISSN号 | 1874-2718 |
| DOI | 10.1007/s12104-017-9795-y |
| 文献子类 | Article |
| 英文摘要 | PhoB is a response regulator of the PhoR/PhoB two-component signal transduction system that is involved in the regulation of the phosphate (Pho) regulon of Escherichia coli. PhoB has two domains, receiver domain and effector domain. The receiver domain can be phosphorylated by its cognate histidine kinase PhoR and the phosphorylation induces conformational changes of the full length protein of PhoB that promote the DNA binding and transcription. Three-dimensional crystal structures of PhoB receiver domain (PhoB(N)) have been solved under apo or BeF3 (-) (a phosphoryl analog) binding forms and it has been found that PhoB(N) is dimerized in both situations. However, we have found that the apo form of PhoB(N) has multiple conformational changes in solution that is hard to be distinguished by using NMR spectroscopy, while the mutagenesis of F20D PhoB(N) gives homogeneous dispersed signals in HSQC spectrum indicating a relatively uniform conformation. Meanwhile the F20D mutant has the same phosphorylation activity as the wild type protein. Here we report the backbone assignment of PhoB(N) (F20D) mutant. The chemical shift (HN, N, CO, C-alpha and C-beta) analysis shows that the predicted regions of secondary structure are in good agreement with those observed in the crystal structure of apo PhoB(N). Therefore, the backbone chemical shifts assignment of PhoB(N) (F20D) mutant would be useful for studying the structure and dynamics of PhoB receiver domain and it has significance for explaining the mechanism of phosphorylation in TCSs. |
| WOS关键词 | RECEIVER DOMAIN ; PHOSPHORYLATION ; DIMERIZATION ; ACTIVATION ; MECHANISM ; NTRC |
| WOS研究方向 | Biophysics ; Spectroscopy |
| 语种 | 英语 |
| WOS记录号 | WOS:000428448100026 |
| 出版者 | SPRINGER |
| 资助机构 | Natural Science Foundation of China(21573280 ; Natural Science Foundation of China(21573280 ; 21603268) ; 21603268) ; Natural Science Foundation of China(21573280 ; Natural Science Foundation of China(21573280 ; 21603268) ; 21603268) ; Natural Science Foundation of China(21573280 ; Natural Science Foundation of China(21573280 ; 21603268) ; 21603268) ; Natural Science Foundation of China(21573280 ; Natural Science Foundation of China(21573280 ; 21603268) ; 21603268) |
| 源URL | [http://ir.wipm.ac.cn/handle/112942/12950]  |
| 专题 | 中国科学院武汉物理与数学研究所 |
| 通讯作者 | Jiang, Ling |
| 作者单位 | 1.Chinese Acad Sci, Grad Univ, 19A Yuquanlu, Beijing 100049, Peoples R China 2.Chinese Acad Sci, Key Lab Magnet Resonance Biol Syst, Natl Ctr Magnet Resonance Wuhan, Wuhan Inst Phys & Math,State Key Lab Magnet Reson, Wuhan 430071, Hubei, Peoples R China |
| 推荐引用方式 GB/T 7714 | Kou, Xinhui,Liu, Xinghong,Liu, Yixiang,et al. Backbone resonance assignment of the response regulator protein PhoB(N) (F20D) from Escherichia coli[J]. BIOMOLECULAR NMR ASSIGNMENTS,2018,12(1):133-137. |
| APA | Kou, Xinhui,Liu, Xinghong,Liu, Yixiang,Li, Conggang,Liu, Maili,&Jiang, Ling.(2018).Backbone resonance assignment of the response regulator protein PhoB(N) (F20D) from Escherichia coli.BIOMOLECULAR NMR ASSIGNMENTS,12(1),133-137. |
| MLA | Kou, Xinhui,et al."Backbone resonance assignment of the response regulator protein PhoB(N) (F20D) from Escherichia coli".BIOMOLECULAR NMR ASSIGNMENTS 12.1(2018):133-137. |
入库方式： OAI收割
来源：武汉物理与数学研究所
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