1. Conformational Dynamics of apo-GlnBP Revealed by Experimental and Computational Analysis.
- Author
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Feng, Yitao, Zhang, Lu, Wu, Shaowen, Liu, Zhijun, Gao, Xin, Zhang, Xu, Liu, Maili, Liu, Jianwei, Huang, Xuhui, and Wang, Wenning
- Subjects
CONFORMATIONAL analysis ,GLUTAMINE ,CARRIER proteins ,CRYSTAL structure ,NUCLEAR magnetic resonance spectroscopy ,COORDINATE covalent bond ,COUPLING reactions (Chemistry) - 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. [ABSTRACT FROM AUTHOR]
- Published
- 2016
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