The Glutamine-Binding Protein (GlnBP) of Escherichia coli is responsible for the first step in the active transport of glutamine across the cytoplasmic membrane. In present work, we explored the allosteric pathway of GlnBP from the open to closed states during the substrate binding process with the adaptive anisotropic network model (aANM). The results show that the allosteric transition proceeds in a coupled way and is more likely to be driven by the movement of hinge regions. The large-scale hinge-bending motion between the large and small domains occurs, accompanied by an interdomain twisting motion which proceeds mainly in the middle stage. The cooperative motion between the dominant hinge-bending motion and the twisting motion exerts a crucial role in the open-closed motions of GlnBP. These results are in close agreement with previous experimental and theoretical data, implying that the topology structure plays a crucial role in the allosteric transition process of GlnBP.

中文翻译：

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预测谷氨酰胺结合蛋白开闭行为的粗粒度方法

大肠杆菌的谷氨酰胺结合蛋白（GlnBP）负责谷氨酰胺跨细胞质膜主动转运的第一步。在目前的工作中，我们使用自适应各向异性网络模型（aANM）探索了底物结合过程中GlnBP从开放状态到封闭状态的变构途径。结果表明，变构过渡以耦合的方式进行，并且更可能由铰链区的运动驱动。发生在大畴和小畴之间的大规模铰链弯曲运动，并伴有主要在中间阶段进行的畴间扭曲运动。主导铰链弯曲运动和扭转运动之间的协同运动在GlnBP的开闭运动中起着至关重要的作用。这些结果与先前的实验和理论数据非常吻合，