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

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    Type
    Article
    Authors
    Feng, Yitao
    Zhang, Lu
    Wu, Shaowen
    Liu, Zhijun
    Gao, Xin cc
    Zhang, Xu
    Liu, Maili
    Liu, Jianwei
    Huang, Xuhui cc
    Wang, Wenning cc
    KAUST Department
    Computational Bioscience Research Center (CBRC)
    Computer Science Program
    Computer, Electrical and Mathematical Sciences and Engineering (CEMSE) Division
    Date
    2016-10-12
    Online Publication Date
    2016-10-12
    Print Publication Date
    2016-11-02
    Permanent link to this record
    http://hdl.handle.net/10754/623162
    
    Metadata
    Show full item record
    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
    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.
    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.
    Publisher
    Wiley
    Journal
    Angewandte Chemie
    DOI
    10.1002/anie.201606613
    10.1002/ange.201606613
    Additional Links
    http://onlinelibrary.wiley.com/doi/10.1002/anie.201606613/abstract
    ae974a485f413a2113503eed53cd6c53
    10.1002/anie.201606613
    Scopus Count
    Collections
    Articles; Computer Science Program; Computational Bioscience Research Center (CBRC); Computer, Electrical and Mathematical Science and Engineering (CEMSE) Division

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