Identification of functionally key residues in maltose transporter with an elastic network model-based thermodynamic method
| Autor: | Jianjun Tan, Chunhua Li, Cunxin Wang, Xiaoyi Zhang, Jiguo Su, Dashuai Lv |
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| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Maltose transport 030102 biochemistry & molecular biology Allosteric regulation Biophysics Substrate (chemistry) Transporter Maltose Condensed Matter Physics medicine.disease_cause Adenosine 03 medical and health sciences chemistry.chemical_compound 030104 developmental biology chemistry Biochemistry medicine Physical and Theoretical Chemistry Signal transduction Molecular Biology Escherichia coli medicine.drug |
| Zdroj: | Molecular Physics. 114:3407-3417 |
| ISSN: | 1362-3028 0026-8976 |
| DOI: | 10.1080/00268976.2016.1234077 |
| Popis: | Periplasmic binding protein-dependent maltose transport system (MBP-MalFGK2) of Escherichia coli, 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-MalFGK2 were considered to be key residues. In result, the key residues in 62 clusters distributed in different subdomains were identified successful... |
| Databáze: | OpenAIRE |
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