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    Maltose-binding protein effectively stabilizes the partially closed conformation of the ATP-binding cassette transporter MalFGK2

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    Type
    Article
    Authors
    Weng, Jingwei
    Gu, Shuo cc
    Gao, Xin cc
    Huang, Xuhui cc
    Wang, Wenning cc
    KAUST Department
    Computational Bioscience Research Center (CBRC)
    Computer Science Program
    Computer, Electrical and Mathematical Sciences and Engineering (CEMSE) Division
    Date
    2017
    Permanent link to this record
    http://hdl.handle.net/10754/623019
    
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    Abstract
    Maltose 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
    Citation
    Weng 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.
    Sponsors
    This 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.
    Publisher
    Royal Society of Chemistry (RSC)
    Journal
    Physical Chemistry Chemical Physics
    DOI
    10.1039/c6cp07943a
    Additional Links
    http://pubs.rsc.org/en/Content/ArticleLanding/2017/CP/C6CP07943A
    ae974a485f413a2113503eed53cd6c53
    10.1039/c6cp07943a
    Scopus Count
    Collections
    Articles; Computer Science Program; Computational Bioscience Research Center (CBRC); Computer, Electrical and Mathematical Science and Engineering (CEMSE) Division

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