Conformational Dynamics of apo-GlnBP Revealed by Experimental and Computational Analysis
Type
ArticleAuthors
Feng, YitaoZhang, Lu
Wu, Shaowen
Liu, Zhijun
Gao, Xin

Zhang, Xu
Liu, Maili
Liu, Jianwei
Huang, Xuhui

Wang, Wenning

KAUST Department
Computational Bioscience Research Center (CBRC)Computer Science Program
Computer, Electrical and Mathematical Sciences and Engineering (CEMSE) Division
Date
2016-10-12Online Publication Date
2016-10-12Print Publication Date
2016-11-02Permanent link to this record
http://hdl.handle.net/10754/623162
Metadata
Show full item recordAbstract
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, WeinheimCitation
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
WileyJournal
Angewandte ChemieAdditional Links
http://onlinelibrary.wiley.com/doi/10.1002/anie.201606613/abstractae974a485f413a2113503eed53cd6c53
10.1002/anie.201606613