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• W2914625024 abstract "Na + /H + antiporters exchange sodium ions (Na + ) and protons (H + ) on opposite sides of lipid membranes, using the gradient of one ion to drive the uphill transport of the other. The electroneutral Na + /H + antiporter NhaP from archaea Pyrococcus abyssi (PaNhaP) is a functional homolog of the human Na + /H + exchanger NHE1, which is an important drug target. Here we resolve the Na + and H + transport cycle of PaNhaP in continuous and unbiased molecular dynamics trajectories that cover the entire transport cycle. We overcome the enormous time-scale gap between seconds-scale ion exchange and microseconds simulations by transition-path shooting. In this way, we selectively capture the rare events in which the six-helix-bundle transporter domain spontaneously moves up and down to shuttle protons and ions across the membrane. The simulations reveal two hydrophobic gates above and below the ion-binding sites that open and close in response to the bundle motion. Weakening the outside gate by mutagenesis makes the transporter faster, suggesting that the gate balances competing demands of fidelity and efficiency. Transition-path sampling and a committor-based reaction coordinate optimization identify the essential motions and interactions that realize conformational alternation between the two access states in transporter function." @default.
• W2914625024 created "2019-02-21" @default.
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• W2914625024 date "2019-02-03" @default.
• W2914625024 modified "2023-09-25" @default.
• W2914625024 title "Mechanism of electroneutral sodium/proton antiporter from transition-path shooting" @default.
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• W2914625024 doi "https://doi.org/10.1101/538777" @default.
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