Crystal structure of the plasma membrane proton pump

Bjørn P. Pedersen, Morten J. Buch-Pedersen, J. Preben Morth, Michael G. Palmgren () and Poul Nissen ()
Additional contact information
Bjørn P. Pedersen: Centre for Membrane Pumps in Cells and Disease—PUMPKIN. Danish National Research Foundation,
Morten J. Buch-Pedersen: Centre for Membrane Pumps in Cells and Disease—PUMPKIN. Danish National Research Foundation,
J. Preben Morth: Centre for Membrane Pumps in Cells and Disease—PUMPKIN. Danish National Research Foundation,
Michael G. Palmgren: Centre for Membrane Pumps in Cells and Disease—PUMPKIN. Danish National Research Foundation,
Poul Nissen: Centre for Membrane Pumps in Cells and Disease—PUMPKIN. Danish National Research Foundation,

Nature, 2007, vol. 450, issue 7172, 1111-1114

Abstract: Pumping Ions P-type ATPases are cation pumps of fundamental importance for all eukaryotes and many prokaryotes. Three papers this week present structural and functional studies of key members of this superfamily. The cover shows the Na+,K+-pump structure, described at 3.5 Å resolution by Morth et al., together with J. C. Skou's original notes on his discovery of its Na+- and K+-dependent ATPase activity 50 years ago. The paper reveals the potassium-bound state and hints at a voltage-dependent basis of regulation, in part through kinetic experiments similar to Skou's. Olesen et al. have obtained crystallographic snapshots of the sarcoplasmic reticulum Ca2+-ATPase, the calcium pump, complemented by functional studies, and a complete mechanism of calcium transport is finally presented. In plants and fungi, cellular ion homeostasis and membrane potential are powered by the plasma membrane H+-ATPase — another P-type ATPase. Pedersen et al. present its X-ray structure and provide insight into how it pumps protons against a steep electrochemical gradient.

Date: 2007
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DOI: 10.1038/nature06417

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