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>