Solid-State NMR Studies of the Succinate-Acetate Permease from Citrobacter Koseri in Liposomes and Native Nanodiscs

doi:10.3390/life11090908

	Solid-State NMR Studies of the Succinate-Acetate Permease from Citrobacter Koseri in Liposomes and Native Nanodiscs
	Dong, Xing-Qi1,2,3 ; Lin, Jing-Yu1,2,3 ; Wang, Peng-Fei1,2,3 ; Li, Yi 1,2,3; Wang, Jian1 ; Li, Bing1 ; Liao, Jun1 ; Lu, Jun-Xia1
	2021-09
发表期刊	LIFE-BASEL
EISSN	2075-1729
卷号	11 期号:9
DOI	10.3390/life11090908
摘要	The succinate-acetate permease (SatP) is an anion channel with six transmembrane domains. It forms different oligomers, especially hexamers in the detergent as well as in the membrane. Solid-state NMR studies of SatP were carried out successfully on SatP complexes by reconstructing the protein into liposomes or retaining the protein in the native membrane of E. coli., where it was expressed. The comparison of C-13-C-13 2D correlation spectra between the two samples showed great similarity, opening the possibility to further study the acetate transport mechanism of SatP in its native membrane environment. Solid-state NMR studies also revealed small chemical shift differences of SatP in the two different membrane systems, indicating the importance of the lipid environment in determining the membrane protein structures and dynamics. Combining different 2D SSNMR spectra, chemical shift assignments were made on some sites, consistent with the helical structures in the transmembrane domains. In the end, we pointed out the limitation in the sensitivity for membrane proteins with such a size, and also indicated possible ways to overcome it.
关键词	membrane protein complex functional state native membrane environment H-1-detected solid-state NMR
URL	查看原文
收录类别	SCIE
语种	英语
WOS研究方向	Life Sciences & Biomedicine - Other Topics ; Microbiology
WOS类目	Biology ; Microbiology
WOS记录号	WOS:000699605600001
出版者	MDPI
原始文献类型	Article
引用统计
文献类型	期刊论文
条目标识符	https://kms.shanghaitech.edu.cn/handle/2MSLDSTB/128342
专题	生命科学与技术学院_博士生生命科学与技术学院_PI研究组_廖军组生命科学与技术学院_PI研究组_陆珺霞组生命科学与技术学院_公共科研平台_分子细胞学平台生命科学与技术学院_硕士生
通讯作者	Lu, Jun-Xia
作者单位	1.ShanghaiTech Univ, Sch Life Sci & Technol, Shanghai 201210, Peoples R China; 2.Chinese Acad Sci, CAS Ctr Excellence Mol Cell Sci, Shanghai Inst Biochem & Cell Biol, State Key Lab Mol Biol, Shanghai 200031, Peoples R China; 3.Univ Chinese Acad Sci, Beijing 100049, Peoples R China
第一作者单位	生命科学与技术学院
通讯作者单位	生命科学与技术学院
第一作者的第一单位	生命科学与技术学院
推荐引用方式 GB/T 7714	Dong, Xing-Qi,Lin, Jing-Yu,Wang, Peng-Fei,et al. Solid-State NMR Studies of the Succinate-Acetate Permease from Citrobacter Koseri in Liposomes and Native Nanodiscs[J]. LIFE-BASEL,2021,11(9).
APA	Dong, Xing-Qi.,Lin, Jing-Yu.,Wang, Peng-Fei.,Li, Yi.,Wang, Jian.,...&Lu, Jun-Xia.(2021).Solid-State NMR Studies of the Succinate-Acetate Permease from Citrobacter Koseri in Liposomes and Native Nanodiscs.LIFE-BASEL,11(9).
MLA	Dong, Xing-Qi,et al."Solid-State NMR Studies of the Succinate-Acetate Permease from Citrobacter Koseri in Liposomes and Native Nanodiscs".LIFE-BASEL 11.9(2021).