Structure and transport mechanism of the sodium/proton antiporter MjNhaP1Batista Paulino, C., Woehlert, D., Karpotova, E., Yildiz, Ö. & Kuehlbrandt, W., 26-Nov-2014, In : eLife. 3, p. 1-21 21 p., e03583.
Research output: Contribution to journal › Article › Academic › peer-review
Sodium/proton antiporters are essential for sodium and pH homeostasis and play a major role in human health and disease. We determined the structures of the archaeal sodium/proton antiporter MjNhaP1 in two complementary states. The inward-open state was obtained by x-ray crystallography in the presence of sodium at pH8, where the transporter is highly active. The outward-open state was obtained by electron crystallography without sodium at pH4, where MjNhaP1 is inactive. Comparison of both structures reveals a 7 degrees tilt of the 6-helix bundle. Na-22(+) uptake measurements indicate non-cooperative transport with an activity maximum at pH7.5. We conclude that binding of a Na+ ion from the outside induces helix movements that close the extracellular cavity, open the cytoplasmic funnel, and result in a similar to 5 angstrom vertical relocation of the ion binding site to release the substrate ion into the cytoplasm.
|Number of pages||21|
|Publication status||Published - 26-Nov-2014|
- Structure, transport, MjNhaP1 antiporter, cryo-EM, single particle analysis
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