Institutional Repository of Chinese Acad Sci, High Field Magnet Lab,Hefei 230031, Anhui, Peoples R China
| Structure of an E. coli integral membrane sulfurtransferase and its structural transition upon SCN- binding defined by EPR-based hybrid method | |
Ling, Shenglong1,2; Wang, Wei1,2 ; Yu, Lu1,2; Peng, Junhui1,2; Cai, Xiaoying1,2; Xiong, Ying1,2; Hayati, Zahra3; Zhang, Longhua1,2; Zhang, Zhiyong1,2; Song, Likai3; Tian, Changlin1,2
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| 2016-01-28 | |
| Source Publication | SCIENTIFIC REPORTS
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| Abstract | 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. |
| Subtype | Article |
| WOS Headings | Science & Technology |
| DOI | 10.1038/srep20025 |
| WOS Keyword | PROTEIN-STRUCTURE DETERMINATION ; CRYSTAL-STRUCTURE ; ESCHERICHIA-COLI ; CONFORMATIONAL DYNAMICS ; SPIN LABELS ; SIDE-CHAINS ; CELL-CYCLE ; CW-EPR ; DOMAIN ; RHODANESE |
| Indexed By | SCI |
| Language | 英语 |
| Funding Organization | 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) |
| WOS Research Area | Science & Technology - Other Topics |
| WOS Subject | Multidisciplinary Sciences |
| WOS ID | WOS:000368783700001 |
| Citation statistics | |
| Document Type | 期刊论文 |
| Identifier | http://ir.hfcas.ac.cn:8080/handle/334002/22236 |
| Collection | 中科院强磁场科学中心 |
| Affiliation | 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 |
| First Author Affilication | Chinese Acad Sci, High Field Magnet Lab,Hefei 230031, Anhui, Peoples R China |
| Recommended Citation 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. |
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| Structure of an E. c（1835KB） | 期刊论文 | 作者接受稿 | 开放获取 | CC BY-NC-SA | View Download | |
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