Structure of an E. coli integral membrane sulfurtransferase and its structural transition upon SCN- binding defined by EPR-based hybrid method

doi:10.1038/srep20025

CORC > 合肥物质科学研究院 > 中国科学院合肥物质科学研究院 > 中科院强磁场科学中心

	Structure of an E. coli integral membrane sulfurtransferase and its structural transition upon SCN- binding defined by EPR-based hybrid method
	Ling, Shenglong 1,2; Wang, Wei 1,2; Yu, Lu 1,2; Peng, Junhui 1,2; Cai, Xiaoying 1,2; Xiong, Ying 1,2; Hayati, Zahra 3; Zhang, Longhua 1,2; Zhang, Zhiyong 1,2; Song, Likai 3
刊名	SCIENTIFIC REPORTS
	2016-01-28
卷号	6 期号:无页码:1-12
DOI	10.1038/srep20025
文献子类	Article
英文摘要	Electron paramagnetic resonance (EPR)-based hybrid experimental and computational approaches were applied to determine the structure of a full-length E. coli integral membrane sulfurtransferase, dimeric YgaP, and its structural and dynamic changes upon ligand binding. The solution NMR structures of the YgaP transmembrane domain (TMD) and cytosolic catalytic rhodanese domain were reported recently, but the tertiary fold of full-length YgaP was not yet available. Here, systematic site-specific EPR analysis defined a helix-loop-helix secondary structure of the YagP-TMD monomers using mobility, accessibility and membrane immersion measurements. The tertiary folds of dimeric YgaP-TMD and full-length YgaP in detergent micelles were determined through inter-and intra-monomer distance mapping and rigid-body computation. Further EPR analysis demonstrated the tight packing of the two YgaP second transmembrane helices upon binding of the catalytic product SCN-, which provides insight into the thiocyanate exportation mechanism of YgaP in the E. coli membrane.
WOS关键词	PROTEIN-STRUCTURE DETERMINATION ; CRYSTAL-STRUCTURE ; ESCHERICHIA-COLI ; CONFORMATIONAL DYNAMICS ; SPIN LABELS ; SIDE-CHAINS ; CELL-CYCLE ; CW-EPR ; DOMAIN ; RHODANESE
WOS研究方向	Science & Technology - Other Topics
语种	英语
WOS记录号	WOS:000368783700001
资助机构	National Key Science Research Grant of Ministry of Science and Technology, China(2015CB910100) ; National Key Science Research Grant of Ministry of Science and Technology, China(2015CB910100) ; National Key Science Research Grant of Ministry of Science and Technology, China(2015CB910100) ; National Key Science Research Grant of Ministry of Science and Technology, China(2015CB910100) ; National Key Science Research Grant of Ministry of Science and Technology, China(2015CB910100) ; National Key Science Research Grant of Ministry of Science and Technology, China(2015CB910100) ; National Key Science Research Grant of Ministry of Science and Technology, China(2015CB910100) ; National Key Science Research Grant of Ministry of Science and Technology, China(2015CB910100) ; National Natural Science Foundation of China(U1332138 ; National Natural Science Foundation of China(U1332138 ; National Natural Science Foundation of China(U1332138 ; National Natural Science Foundation of China(U1332138 ; National Natural Science Foundation of China(U1332138 ; National Natural Science Foundation of China(U1332138 ; National Natural Science Foundation of China(U1332138 ; National Natural Science Foundation of China(U1332138 ; U.S. National High Magnetic Field Laboratory (NHFML)(5080) ; U.S. National High Magnetic Field Laboratory (NHFML)(5080) ; U.S. National High Magnetic Field Laboratory (NHFML)(5080) ; U.S. National High Magnetic Field Laboratory (NHFML)(5080) ; U.S. National High Magnetic Field Laboratory (NHFML)(5080) ; U.S. National High Magnetic Field Laboratory (NHFML)(5080) ; U.S. National High Magnetic Field Laboratory (NHFML)(5080) ; U.S. National High Magnetic Field Laboratory (NHFML)(5080) ; State of Florida ; State of Florida ; State of Florida ; State of Florida ; State of Florida ; State of Florida ; State of Florida ; State of Florida ; U.S. National Science Foundation(DMR-1157490) ; U.S. National Science Foundation(DMR-1157490) ; U.S. National Science Foundation(DMR-1157490) ; U.S. National Science Foundation(DMR-1157490) ; U.S. National Science Foundation(DMR-1157490) ; U.S. National Science Foundation(DMR-1157490) ; U.S. National Science Foundation(DMR-1157490) ; U.S. National Science Foundation(DMR-1157490) ; 21473176) ; 21473176) ; 21473176) ; 21473176) ; 21473176) ; 21473176) ; 21473176) ; 21473176) ; National Key Science Research Grant of Ministry of Science and Technology, China(2015CB910100) ; National Key Science Research Grant of Ministry of Science and Technology, China(2015CB910100) ; National Key Science Research Grant of Ministry of Science and Technology, China(2015CB910100) ; National Key Science Research Grant of Ministry of Science and Technology, China(2015CB910100) ; National Key Science Research Grant of Ministry of Science and Technology, China(2015CB910100) ; National Key Science Research Grant of Ministry of Science and Technology, China(2015CB910100) ; National Key Science Research Grant of Ministry of Science and Technology, China(2015CB910100) ; National Key Science Research Grant of Ministry of Science and Technology, China(2015CB910100) ; National Natural Science Foundation of China(U1332138 ; National Natural Science Foundation of China(U1332138 ; National Natural Science Foundation of China(U1332138 ; National Natural Science Foundation of China(U1332138 ; National Natural Science Foundation of China(U1332138 ; National Natural Science Foundation of China(U1332138 ; National Natural Science Foundation of China(U1332138 ; National Natural Science Foundation of China(U1332138 ; U.S. National High Magnetic Field Laboratory (NHFML)(5080) ; U.S. National High Magnetic Field Laboratory (NHFML)(5080) ; U.S. National High Magnetic Field Laboratory (NHFML)(5080) ; U.S. National High Magnetic Field Laboratory (NHFML)(5080) ; U.S. National High Magnetic Field Laboratory (NHFML)(5080) ; U.S. National High Magnetic Field Laboratory (NHFML)(5080) ; U.S. National High Magnetic Field Laboratory (NHFML)(5080) ; U.S. National High Magnetic Field Laboratory (NHFML)(5080) ; State of Florida ; State of Florida ; State of Florida ; State of Florida ; State of Florida ; State of Florida ; State of Florida ; State of Florida ; U.S. National Science Foundation(DMR-1157490) ; U.S. National Science Foundation(DMR-1157490) ; U.S. National Science Foundation(DMR-1157490) ; U.S. National Science Foundation(DMR-1157490) ; U.S. National Science Foundation(DMR-1157490) ; U.S. National Science Foundation(DMR-1157490) ; U.S. National Science Foundation(DMR-1157490) ; U.S. National Science Foundation(DMR-1157490) ; 21473176) ; 21473176) ; 21473176) ; 21473176) ; 21473176) ; 21473176) ; 21473176) ; 21473176)
内容类型	期刊论文
源URL	[http://ir.hfcas.ac.cn:8080/handle/334002/22236]
专题	合肥物质科学研究院_中科院强磁场科学中心
作者单位	1.Univ Sci & Technol China, Natl Lab Phys Sci Microscale, Sch Life Sci, Hefei 230027, Peoples R China 2.Chinese Acad Sci, High Field Magnet Lab, Hefei 230027, Peoples R China 3.Florida State Univ, Natl High Magnet Field Lab, Tallahassee, FL 32310 USA
推荐引用方式 GB/T 7714	Ling, Shenglong,Wang, Wei,Yu, Lu,et al. Structure of an E. coli integral membrane sulfurtransferase and its structural transition upon SCN- binding defined by EPR-based hybrid method[J]. SCIENTIFIC REPORTS,2016,6(无):1-12.
APA	Ling, Shenglong.,Wang, Wei.,Yu, Lu.,Peng, Junhui.,Cai, Xiaoying.,...&Tian, Changlin.(2016).Structure of an E. coli integral membrane sulfurtransferase and its structural transition upon SCN- binding defined by EPR-based hybrid method.SCIENTIFIC REPORTS,6(无),1-12.
MLA	Ling, Shenglong,et al."Structure of an E. coli integral membrane sulfurtransferase and its structural transition upon SCN- binding defined by EPR-based hybrid method".SCIENTIFIC REPORTS 6.无(2016):1-12.