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

28 Scopus citations

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
Original languageEnglish (US)
Pages (from-to)13990-13994
Number of pages5
JournalAngewandte Chemie International Edition
Volume55
Issue number45
DOIs
StatePublished - Oct 12 2016

Bibliographical note

KAUST Repository Item: Exported on 2020-10-01
Acknowledgements: 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.

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