Journal
FEBS LETTERS
Volume 585, Issue 22, Pages 3533-3537Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2011.10.015
Keywords
Membrane protein; Nanodisc; Lipid-protein interaction; Membrane model system; ABC-transporter
Funding
- Japan Society for the Promotion of Science
- Grants-in-Aid for Scientific Research [21360398] Funding Source: KAKEN
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ATP-binding cassette (ABC) transporters couple hydrolysis of ATP with vectorial transport across the cell membrane. We have reconstituted ABC transporter MsbA in nanodiscs of various sizes and lipid compositions to test whether ATPase activity is modulated by the properties of the bilayer. ATP hydrolysis rates, Michaelis-Menten parameters, and dissociation constants of substrate analog ATP-gamma-S demonstrated that physicochemical properties of the bilayer modulated binding and ATPase activity. This is remarkable when considering that the catalytic unit is located similar to 50 angstrom from the transmembrane region. Our results validated the use of nanodiscs as an effective tool to reconstitute MsbA in an active catalytic state, and highlighted the close relationship between otherwise distant transmembrane and ATPase modules. (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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