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- W2953345709 abstract "The multidrug transporter AcrB transports a broad range of drugs out of the cell by means of the proton-motive force. The asymmetric crystal structure of trimeric AcrB suggests a functionally rotating mechanism for drug transport. Despite various supportive evidences from biochemical and simulation studies for this mechanism, the link between the functional rotation and proton translocation across the membrane remains elusive. Here, calculating the minimum free energy pathway of the functional rotation for the complete AcrB trimer, we describe the structural and energetic basis behind the coupling between the functional rotation and the proton translocation at atomic-level. Free energy calculations show that protonation of Asp408 in the transmembrane portion of the drug-bound protomer drives the functional rotation. The conformational pathway identifies vertical shear motions among several transmembrane helices, which regulates alternate access of water in the transmembrane as well as peristaltic motions pumping drugs in the periplasm." @default.
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- W2953345709 date "2017-08-08" @default.
- W2953345709 modified "2023-10-02" @default.
- W2953345709 title "Energetics and Conformational Pathways of Functional Rotation in the Multidrug Transporter AcrB" @default.
- W2953345709 doi "https://doi.org/10.1101/173567" @default.
- W2953345709 hasPublicationYear "2017" @default.
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