Journal article
Negative stain single-particle em of the maltose transporter in nanodiscs reveals asymmetric closure of MalK2 and catalytic roles of ATP, MalE, and maltose
L Fabre, H Bao, J Innes, F Duong, I Rouiller
Journal of Biological Chemistry | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | Published : 2017
Abstract
The Escherichia coli MalE-MalFGK2 complex is one of the best characterized members of the large and ubiquitous family of ATP-binding cassette (ABC) transporters. It is composed of a membrane-spanning heterodimer, MalF-MalG; a homodimeric ATPase, MalK2; and a periplasmic maltose receptor, MalE. Opening and closure of MalK2 is coupled to conformational changes in MalF-MalG and the alternate exposition of the substrate-binding site to either side of the membrane. To further define this alternate access mechanism and the impact of ATP, MalE, and maltose on the conformation of the transporter during the transport cycle, we have reconstituted MalFGK2 in nanodiscs and analyzed its conformations und..
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Awarded by Canadian Institutes of Health Research
Funding Acknowledgements
This work was supported by Canadian Institutes of Health Research Grants 86693MOP (to I. R.) and 74525MOP (to F. D.), the Natural Sciences and Engineering Research Council of Canada Grant RGPIN-2014-04798 (to I. R.), a Bourse de Prestige from the Groupe d'Etude des Proteines Membranaires (which is supported by the Fonds de la Recherche en Sante du Quebec) (to L. F.), and a summer fellowship from the Natural Sciences and Engineering Research Council of Canada Create Training Program in Bionanomachines (to J. I.). The authors declare that they have no conflicts of interest with the contents of this article.