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Dissecting the Protein Dynamics Coupled Ligand Binding with Kinetic Models and Single-Molecule FRET

文献类型： 外文期刊

作者： Wu, Shaowen 1 ; Zhang, Wenyang 1 ; Li, Wenyan 1 ; Huang, Wenjie 1 ; Kong, Qian 1 ; Chen, Zhongjian 1 ; Wei, Wenkang 1 ; Yan, Shijuan 1 ;

作者机构： 1.Guangdong Acad Agr Sci, Guangdong Key Lab Crop Germplasm Resources Preser, Agrobiol Gene Res Ctr, Guangzhou 510640, Guangdong, Peoples R China

期刊名称：BIOCHEMISTRY （ 影响因子：3.321； 五年影响因子：3.261 ）

ISSN： 0006-2960

年卷期： 2022 年 61 卷 6 期

页码：

收录情况： SCI

摘要： Protein-ligand interactions are crucial to many biological processes. Ligand binding and dissociation are the basic steps that allow proteins to function. Protein conformational dynamics have been shown to play important roles in ligand binding and dissociation. However, it is challenging to determine the ligand binding kinetics of dynamic proteins. Here, we undertook comprehensive single-molecule FRET (smFRET) measurements and kinetic model analysis to characterize the conformational dynamics coupled ligand binding of glutamine-binding protein (GlnBP). We showed that hinge and T118A mutations of GlnBP affect its conformational dynamics as well as the ligand binding affinity. Based on smFRET measurements, the kinetic model of ligand-GlnBP interactions was constructed. Using experimentally measured parameters, we solved the rate equations of the model and obtained the undetectable parameters of the model which allowed us to understand the ligand binding kinetics fully. Our results demonstrate that modulation of the conformational dynamics of GlnBP affects the ligand binding and dissociation rates. This study provides insights into the binding kinetics of ligands, which are related to the protein function itself.

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