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Escherichia coli NhaA is a prototype sodium-proton antiporter, which has been extensively characterized by X-ray crystallography, biochemical and biophysical experiments. However, the identities of proton carriers and details of pH-regulated

Escherichia coli NhaA is a prototype sodium-proton antiporter, which has been extensively characterized by X-ray crystallography, biochemical and biophysical experiments. However, the identities of proton carriers and details of pH-regulated mechanism remain controversial. Here we report constant pH molecular dynamics data, which reveal that NhaA activation involves a net charge switch of a pH sensor at the entrance of the cytoplasmic funnel and opening of a hydrophobic gate at the end of the funnel. The latter is triggered by charging of Asp164, the first proton carrier.

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    Date Created
    • 2016-10-06
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    • Digital object identifier: 10.1038/ncomms12940
    • Identifier Type
      International standard serial number
      Identifier Value
      2041-1723
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    Huang, Y., Chen, W., Dotson, D. L., Beckstein, O., & Shen, J. (2016). Mechanism of pH-dependent activation of the sodium-proton antiporter NhaA. Nature Communications, 7, 12940. doi:10.1038/ncomms12940

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