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dc.contributor.authorWeng, Jingwei
dc.contributor.authorGu, Shuo
dc.contributor.authorGao, Xin
dc.contributor.authorHuang, Xuhui
dc.contributor.authorWang, Wenning
dc.date.accessioned2017-03-19T13:24:05Z
dc.date.available2017-03-19T13:24:05Z
dc.date.issued2017
dc.identifier.citationWeng J, Gu S, Gao X, Huang X, Wang W (2017) Maltose-binding protein effectively stabilizes the partially closed conformation of the ATP-binding cassette transporter MalFGK2. Phys Chem Chem Phys. Available: http://dx.doi.org/10.1039/c6cp07943a.
dc.identifier.issn1463-9076
dc.identifier.issn1463-9084
dc.identifier.doi10.1039/c6cp07943a
dc.identifier.urihttp://hdl.handle.net/10754/623019
dc.description.abstractMaltose transporter MalFGK2 is a type-I importer in the ATP-binding cassette (ABC) transporter superfamily. Upon the binding of its periplasmic binding protein, MalE, the ATPase activity of MalFGK2 can be greatly enhanced. Crystal structures of the MalFGK2-MalE-maltose complex in a so-called
dc.description.sponsorshipThis work was supported by National Major Basic Research Program of China (2016YFA0501702), National Science Foundation of China (21473034, 21403036), and Specialized Research Fund for the Doctoral Program of Higher Education (20130071140004). X. H. acknowledges the Hong Kong Research Grants Council (M-HKUST601/13, 609813, 16302214, 16304215, and HKUST C6009-15G). X. G. thanks the support by funding from King Abdullah University of Science and Technology (KAUST). This research made use of the resources of the computer clusters at KAUST and the super computer center at Fudan University.
dc.publisherRoyal Society of Chemistry (RSC)
dc.relation.urlhttp://pubs.rsc.org/en/Content/ArticleLanding/2017/CP/C6CP07943A
dc.rightsArchived with thanks to Phys. Chem. Chem. Phys.
dc.titleMaltose-binding protein effectively stabilizes the partially closed conformation of the ATP-binding cassette transporter MalFGK2
dc.typeArticle
dc.contributor.departmentComputational Bioscience Research Center (CBRC)
dc.contributor.departmentComputer Science Program
dc.contributor.departmentComputer, Electrical and Mathematical Sciences and Engineering (CEMSE) Division
dc.identifier.journalPhys. Chem. Chem. Phys.
dc.eprint.versionPost-print
dc.contributor.institutionShanghai Key Laboratory of Molecular Catalysis and Innovative Materials, Department of Chemistry, and Institutes of Biomedical Sciences, Fudan University, Shanghai, P. R. China.
dc.contributor.institutionDepartment of Chemistry, Institute for Advance Study and School of Science, The Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong, China.
kaust.personGao, Xin
refterms.dateFOA2018-02-23T00:00:00Z


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