Conformational Dynamics of apo-GlnBP Revealed by Experimental and Computational Analysis

Handle URI:
http://hdl.handle.net/10754/623162
Title:
Conformational Dynamics of apo-GlnBP Revealed by Experimental and Computational Analysis
Authors:
Feng, Yitao; Zhang, Lu; Wu, Shaowen; Liu, Zhijun; Gao, Xin ( 0000-0002-7108-3574 ) ; Zhang, Xu; Liu, Maili; Liu, Jianwei; Huang, Xuhui; Wang, Wenning
Abstract:
The glutamine binding protein (GlnBP) binds l-glutamine and cooperates with its cognate transporters during glutamine uptake. Crystal structure analysis has revealed an open and a closed conformation for apo- and holo-GlnBP, respectively. However, the detailed conformational dynamics have remained unclear. Herein, we combined NMR spectroscopy, MD simulations, and single-molecule FRET techniques to decipher the conformational dynamics of apo-GlnBP. The NMR residual dipolar couplings of apo-GlnBP were in good agreement with a MD-derived structure ensemble consisting of four metastable states. The open and closed conformations are the two major states. This four-state model was further validated by smFRET experiments and suggests the conformational selection mechanism in ligand recognition of GlnBP. © 2016 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim
KAUST Department:
Computational Bioscience Research Center (CBRC); Computer, Electrical and Mathematical Sciences and Engineering (CEMSE) Division
Citation:
Feng Y, Zhang L, Wu S, Liu Z, Gao X, et al. (2016) Conformational Dynamics of apo-GlnBP Revealed by Experimental and Computational Analysis. Angewandte Chemie International Edition 55: 13990–13994. Available: http://dx.doi.org/10.1002/anie.201606613.
Publisher:
Wiley-Blackwell
Journal:
Angewandte Chemie International Edition
Issue Date:
13-Oct-2016
DOI:
10.1002/anie.201606613; 10.1002/ange.201606613
Type:
Article
ISSN:
1433-7851
Sponsors:
This work was supported by the National Major Basic Research Program of China (2016YFA0501702), the National Science Foundation of China (21473034, 21273188), and the Specialized Research Fund for the Doctoral Program of Higher Education (20130071140004). X.H. acknowledges the Hong Kong Research Grants Council (M-HKUST601/13, 609813, 16302214, 16304215, and HKUST C6009-15G). X.G. acknowledges funding from King Abdullah University of Science and Technology (KAUST). We thank Dr. Charles D. Schwieters for insightful discussions and the facility team members for their help with NMR experiments at the National Center for Protein Science Shanghai (NCPSS). This research made use of the computer cluster resources at KAUST.
Additional Links:
http://onlinelibrary.wiley.com/doi/10.1002/anie.201606613/abstract
Appears in Collections:
Articles; Computational Bioscience Research Center (CBRC); Computer, Electrical and Mathematical Sciences and Engineering (CEMSE) Division

Full metadata record

DC FieldValue Language
dc.contributor.authorFeng, Yitaoen
dc.contributor.authorZhang, Luen
dc.contributor.authorWu, Shaowenen
dc.contributor.authorLiu, Zhijunen
dc.contributor.authorGao, Xinen
dc.contributor.authorZhang, Xuen
dc.contributor.authorLiu, Mailien
dc.contributor.authorLiu, Jianweien
dc.contributor.authorHuang, Xuhuien
dc.contributor.authorWang, Wenningen
dc.date.accessioned2017-04-13T11:50:58Z-
dc.date.available2017-04-13T11:50:58Z-
dc.date.issued2016-10-13en
dc.identifier.citationFeng Y, Zhang L, Wu S, Liu Z, Gao X, et al. (2016) Conformational Dynamics of apo-GlnBP Revealed by Experimental and Computational Analysis. Angewandte Chemie International Edition 55: 13990–13994. Available: http://dx.doi.org/10.1002/anie.201606613.en
dc.identifier.issn1433-7851en
dc.identifier.doi10.1002/anie.201606613en
dc.identifier.doi10.1002/ange.201606613en
dc.identifier.urihttp://hdl.handle.net/10754/623162-
dc.description.abstractThe glutamine binding protein (GlnBP) binds l-glutamine and cooperates with its cognate transporters during glutamine uptake. Crystal structure analysis has revealed an open and a closed conformation for apo- and holo-GlnBP, respectively. However, the detailed conformational dynamics have remained unclear. Herein, we combined NMR spectroscopy, MD simulations, and single-molecule FRET techniques to decipher the conformational dynamics of apo-GlnBP. The NMR residual dipolar couplings of apo-GlnBP were in good agreement with a MD-derived structure ensemble consisting of four metastable states. The open and closed conformations are the two major states. This four-state model was further validated by smFRET experiments and suggests the conformational selection mechanism in ligand recognition of GlnBP. © 2016 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheimen
dc.description.sponsorshipThis work was supported by the National Major Basic Research Program of China (2016YFA0501702), the National Science Foundation of China (21473034, 21273188), and the Specialized Research Fund for the Doctoral Program of Higher Education (20130071140004). X.H. acknowledges the Hong Kong Research Grants Council (M-HKUST601/13, 609813, 16302214, 16304215, and HKUST C6009-15G). X.G. acknowledges funding from King Abdullah University of Science and Technology (KAUST). We thank Dr. Charles D. Schwieters for insightful discussions and the facility team members for their help with NMR experiments at the National Center for Protein Science Shanghai (NCPSS). This research made use of the computer cluster resources at KAUST.en
dc.publisherWiley-Blackwellen
dc.relation.urlhttp://onlinelibrary.wiley.com/doi/10.1002/anie.201606613/abstracten
dc.subjectconformational dynamicsen
dc.subjectFRETen
dc.subjectmolecular dynamicsen
dc.subjectNMR spectroscopyen
dc.subjectprotein foldingen
dc.titleConformational Dynamics of apo-GlnBP Revealed by Experimental and Computational Analysisen
dc.typeArticleen
dc.contributor.departmentComputational Bioscience Research Center (CBRC)en
dc.contributor.departmentComputer, Electrical and Mathematical Sciences and Engineering (CEMSE) Divisionen
dc.identifier.journalAngewandte Chemie International Editionen
dc.contributor.institutionShanghai Key Laboratory of Molecular Catalysis and Innovative Materials, Department of Chemistry, and Institutes of Biomedical Sciences, Fudan University, Shanghai, Chinaen
dc.contributor.institutionDepartment of Chemistry, The Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kongen
dc.contributor.institutionNational Center for Protein Science, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, Shanghai, Chinaen
dc.contributor.institutionKey Laboratory of Magnetic and Resonance in Biological Systems, State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, Centre for Magnetic Resonance, Wuhan Institute of Physics and Mathematics, Chinese Academy of Sciences, Wuhan, Chinaen
dc.contributor.institutionDivision of Biomedical Engineering, Center of Systems Biology and Human Health, Institute for Advance Study and School of Science, The Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kongen
kaust.authorGao, Xinen
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