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

Yitao Feng, Lu Zhang, Shaowen Wu, Zhijun Liu, Xin Gao, Xu Zhang, Maili Liu, Jianwei Liu, Xuhui Huang, Wenning Wang

Research output: Contribution to journalArticlepeer-review

25 Scopus citations


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
Original languageEnglish (US)
Pages (from-to)13990-13994
Number of pages5
JournalAngewandte Chemie International Edition
Issue number45
StatePublished - Oct 12 2016


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