Maltose-binding protein effectively stabilizes the partially closed conformation of the ATP-binding cassette transporter MalFGK2
Type
Article
KAUST Department
Computational Bioscience Research Center (CBRC)Computer Science Program
Computer, Electrical and Mathematical Sciences and Engineering (CEMSE) Division
Date
2017-02-23Permanent link to this record
http://hdl.handle.net/10754/623019Metadata
Show full item recordAbstract
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-calledCitation
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
Phys. Chem. Chem. Phys.ISSN
1463-90761463-9084