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- W2204708969 abstract "ATP-binding cassette exporters use the energy of ATP hydrolysis to transport substrates across membranes by switching between inward- and outward-facing conformations. Essentially all structural studies of these proteins have been performed with the proteins in detergent micelles, locked in specific conformations and/or at low temperature. Here, we used luminescence resonance energy transfer spectroscopy to study the prototypical ATP-binding cassette exporter MsbA reconstituted in nanodiscs at 37 °C while it performs ATP hydrolysis. We found major differences when comparing MsbA in these native-like conditions with double electron-electron resonance data and the crystal structure of MsbA in the open inward-facing conformation. The most striking differences include a significantly smaller separation between the nucleotide-binding domains and a larger fraction of molecules with associated nucleotide-binding domains in the nucleotide-free apo state. These studies stress the importance of studying membrane proteins in an environment that approaches physiological conditions." @default.
- W2204708969 created "2016-06-24" @default.
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- W2204708969 date "2016-02-01" @default.
- W2204708969 modified "2023-10-14" @default.
- W2204708969 title "The Lipid Bilayer Modulates the Structure and Function of an ATP-binding Cassette Exporter" @default.
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- W2204708969 doi "https://doi.org/10.1074/jbc.m115.698498" @default.
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