10.6084/m9.figshare.3848655.v1 Dashuai Lv Dashuai Lv Chunhua Li Chunhua Li Jianjun Tan Jianjun Tan Xiaoyi Zhang Xiaoyi Zhang Cunxin Wang Cunxin Wang Jiguo Su Jiguo Su Identification of functionally key residues in maltose transporter with an elastic network model-based thermodynamic method Taylor & Francis Group 2016 Maltose transporter thermodynamic cycle key residues elastic network model long-range coupling 2016-09-22 17:11:31 Dataset https://tandf.figshare.com/articles/dataset/Identification_of_functionally_key_residues_in_maltose_transporter_with_an_elastic_network_model-based_thermodynamic_method/3848655 <p>Periplasmic binding protein-dependent maltose transport system (MBP-MalFGK<sub>2</sub>) of <i>Escherichia coli</i>, an important member of the Adenosine triphosphate-binding cassette transporter superfamily, is in charge of the transportation of maltoses across cellular membrane. Studies have shown that this transport processes are activated by the binding of maltose and are accompanied by large-scale cooperative movements between different domains which are mediated by a network of important residues related to signal transduction and allosteric regulation. In this paper, the functionally crucial residues and long-range allosteric pathway of the regulation of the system by substrate were identified by utilising a coarse-grained thermodynamic method proposed by our group. The residues whose perturbations markedly change the binding free energy between maltoses and MBP-MalFGK<sub>2</sub> were considered to be key residues. In result, the key residues in 62 clusters distributed in different subdomains were identified successfully, and the results from our calculation are highly consistent with experimental and theoretical observations. Furthermore, we explored the long-range cooperation within the transporter. These studies will help us better understand the physical mechanism of the effects of the maltose on MBP-MalFGK<sub>2</sub> by long-range allosteric modulation.</p> <p></p>