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Published Online August 8, 2002
Science DOI: 10.1126/science.1072574

Reports

Submitted on April 5, 2002
Accepted on July 25, 2002

Structure, Mechanism, and Regulation of the Neurospora Plasma Membrane H+-ATPase

Werner Kühlbrandt 1, Johan Zeelen 1, Jens Dietrich 2

1 Max-Planck-Institut für Biophysik, Heinrich-Hoffmann-Str. 7, 60528 Frankfurt am Main, Germany.
2 Laboratory of Molecular Biophysics, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.

ATP-driven proton pumps in the plasma membrane of plants and yeasts maintain the intracellular pH and membrane potential. To gain insight into the molecular mechanisms of proton pumping, we built an atomic homology model of the proton pump, based on the 2.6Å x-ray structure of the related Ca2+-ATPase from rabbit sarcoplasmic reticulum, and fitted it to an electron-microscopic 8Å map of the Neurospora H+-ATPase. The model reveals the likely path of the proton through the membrane and shows that the nucleotide-binding domain rotates by ~70° to deliver ATP to the phosphorylation site. A synthetic peptide corresponding to the C-terminal regulatory domain stimulates ATPase activity, suggesting a mechanism for proton transport regulation.


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