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Structure, Mechanism, and Regulation of the Neurospora Plasma Membrane $H^{+}-ATPase$

Werner Kühlbrandt, Johan Zeelen and Jens Dietrich
Science
New Series, Vol. 297, No. 5587 (Sep. 6, 2002), pp. 1692-1696
Stable URL: http://www.jstor.org/stable/3832325
Page Count: 5
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Structure, Mechanism, and Regulation of the Neurospora Plasma Membrane $H^{+}-ATPase$
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Abstract

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 2.6 angstrom x-ray structure of the related Ca2+ pump from rabbit sarcoplasmic reticulum. The model, when fitted to an 8 angstrom map of the Neurospora proton pump determined by electron microscopy, reveals the likely path of the proton through the membrane and shows that the nucleotide-binding domain rotates by $\sim 70\textdegree$ to deliver adenosine triphosphate (ATP) to the phosphorylation site. A synthetic peptide corresponding to the carboxyl-terminal regulatory domain stimulates ATPase activity, suggesting a mechanism for proton transport regulation.

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