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

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• 作者：Yitao Feng ; Lu Zhang ; Shaowen Wu ; Zhijun Liu ; Xin Gao ; Xu Zhang ; Maili Liu ; Jianwei Liu ; Xuhui Huang and Wenning Wang
• 刊名：Angewandte Chemie
• 出版年：2016
• 出版时间：November 2, 2016
• 年：2016
• 卷：128
• 期：45
• 页码：14196-14200
• 全文大小：2388K
• ISSN：1521-3757

文摘

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.