Conformational Dynamics of apo‐GlnBP Revealed by Experimental and Computational Analysis |
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| Authors: | Yitao Feng Lu Zhang Shaowen Wu Zhijun Liu Xin Gao Xu Zhang Maili Liu Jianwei Liu Xuhui Huang Wenning Wang |
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| Affiliation: | 1. Shanghai Key Laboratory of Molecular Catalysis and Innovative Materials, Department of Chemistry, and Institutes of Biomedical Sciences, Fudan University, Shanghai, P.R. China;2. Department of Chemistry, The Hong Kong University of Science and Technology, Kowloon, Hong Kong;3. National Center for Protein Science, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, Shanghai, China;4. King Abdullah University of Science and Technology (KAUST), Computational Bioscience Research Center (CBRC), Computer, Electrical and Mathematical Sciences and Engineering (CEMSE) Division, Thuwal, Saudi Arabia;5. Key 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, China;6. Division 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, Kowloon, Hong Kong |
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| 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. |
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| Keywords: | conformational dynamics FRET molecular dynamics NMR spectroscopy protein folding |
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