Maltose-binding protein effectively stabilizes the partially closed conformation of the ATP-binding cassette transporter MalFGK2
KAUST DepartmentComputational Bioscience Research Center (CBRC)
Computer Science Program
Computer, Electrical and Mathematical Sciences and Engineering (CEMSE) Division
Permanent link to this recordhttp://hdl.handle.net/10754/623019
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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
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.
SponsorsThis 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.
PublisherRoyal Society of Chemistry (RSC)
JournalPhys. Chem. Chem. Phys.