Dimerization and Conformational Exchanges of the Receiver Domain of Response Regulator PhoB from Escherichia coli

doi:10.1021/acs.jpcb.8b01034

CORC > 武汉物理与数学研究所 > 中国科学院武汉物理与数学研究所 > 磁共振基础研究部

	Dimerization and Conformational Exchanges of the Receiver Domain of Response Regulator PhoB from Escherichia coli
	Liu, Yixiang 2; Li, Conggang 2; Liu, Maili 2; Jiang, Ling 2; Kou, Xinhui 1,2
刊名	JOURNAL OF PHYSICAL CHEMISTRY B
	2018-06-07
卷号	122 期号:22 页码:5749-5757
DOI	10.1021/acs.jpcb.8b01034
文献子类	Article
英文摘要	PhoB is a response regulator of PhoR/PhoB two-component system from Escherichia coli that is involved in the environmental phosphate regulation. It has been reported that the N-terminal receiver domain (PhoB(N)) forms a dimer using the alpha 1-alpha 5 face in the apo state and a dimer using the alpha 4-beta 5-alpha 5 face in the active state investigated by X-ray crystallography. However, it is not clear whether the conformational switch of the dimer is dependent on phosphorylation. Here, we report the NMR studies of PhoB(N) in solution in its apo form. We observed that the secondary structural fragments of apo PhoB(N) characterized by NMR are almost the same as those determined by crystallography, but the NMR spectrum of PhoB(N) shows inhomogeneous amide signals. Concentration dilution experiments and backbone relaxation parameters showed that PhoB(N) exists in equilibrium between monomer and dimer states. Using paramagnetic relaxation enhancement experiments, we demonstrated that the dimer of apo PhoB(N) forms several transient dimer interfaces in solution. This finding suggested that, in addition to the monomer-to-dimer exchange, the inactive conformation of PhoB(N) has different domain arrangements, which are independent of phosphorylation. It provides an experimental data for the conformational selection mechanism of the phosphorylation of PhoB(N).
WOS关键词	PARAMAGNETIC RELAXATION ENHANCEMENT ; MYCOBACTERIUM-TUBERCULOSIS ; SIGNAL-TRANSDUCTION ; OMPR/PHOB SUBFAMILY ; STRUCTURAL-ANALYSIS ; BACKBONE DYNAMICS ; CRYSTAL-STRUCTURE ; NMR-SPECTROSCOPY ; 2-COMPONENT ; MACROMOLECULES
WOS研究方向	Chemistry
语种	英语
WOS记录号	WOS:000435019600003
资助机构	National Key R&D Program of China(2017YFA0505400) ; National Key R&D Program of China(2017YFA0505400) ; National Science Foundation of China(21573280 ; National Science Foundation of China(21573280 ; 21603268) ; 21603268) ; National Key R&D Program of China(2017YFA0505400) ; National Key R&D Program of China(2017YFA0505400) ; National Science Foundation of China(21573280 ; National Science Foundation of China(21573280 ; 21603268) ; 21603268)
内容类型	期刊论文
源URL	[http://ir.wipm.ac.cn/handle/112942/11978]
专题	武汉物理与数学研究所_磁共振基础研究部
作者单位	1.Chinese Acad Sci, Grad Univ, 19A Yuquanlu, 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,Li, Conggang,Liu, Maili,et al. Dimerization and Conformational Exchanges of the Receiver Domain of Response Regulator PhoB from Escherichia coli[J]. JOURNAL OF PHYSICAL CHEMISTRY B,2018,122(22):5749-5757.
APA	Liu, Yixiang,Li, Conggang,Liu, Maili,Jiang, Ling,&Kou, Xinhui.(2018).Dimerization and Conformational Exchanges of the Receiver Domain of Response Regulator PhoB from Escherichia coli.JOURNAL OF PHYSICAL CHEMISTRY B,122(22),5749-5757.
MLA	Liu, Yixiang,et al."Dimerization and Conformational Exchanges of the Receiver Domain of Response Regulator PhoB from Escherichia coli".JOURNAL OF PHYSICAL CHEMISTRY B 122.22(2018):5749-5757.