The fundamental forces of ATP-driven membrane transport (A13#)

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ATP-binding cassette (ABC) transporters are essential membrane proteins found in both eukaryotic and bacterial cells that facilitate the uphill transport of chemically diverse compounds. The molecular details of mechanochemical coupling of ATP-hydrolysis to conformational changes in those proteins remain to be elucidated. We here propose to study two ABC model systems with a combination of single-molecule fluorescence and force spectroscopy to characterize how the ATP-driven motor domain generates and transmits forces. With this we will unravel how chemical energy is converted into conformational changes of the pump domain that drive active transport.