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J. Biol. Chem., Vol. 277, Issue 15, 13115-13121, April 12, 2002

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Three-dimensional Map of a Plant V-ATPase Based on Electron Microscopy^*

Ines Domgall, David Venzke, Ulrich Lüttge^§, Rafael Ratajczak^§, and Bettina Böttcher^¶

From the  Structural and Computational Biology Programme, EMBL, Meyerhofstrasse 1, 69117 Heidelberg and ^§ Institute of Botany, Darmstadt University of Technology, Schnittspahnstrasse 3-5, 64287 Darmstadt, Germany

V-ATPases pump protons into the interior of various subcellular compartments at the expense of ATP. Previous studies have shown that these pumps comprise a membrane-integrated, proton-translocating (V₀), and a soluble catalytic (V₁) subcomplex connected to one another by a thin stalk region. We present two three-dimensional maps derived from electron microscopic images of the complete V-ATPase complex from the plant Kalanchoë daigremontiana at a resolution of 2.2 nm. In the presence of a non-hydrolyzable ATP analogue, the details of the stalk region between V₀ and V₁ were revealed for the first time in their three-dimensional organization. A central stalk was surrounded by three peripheral stalks of different sizes and shapes. In the absence of the ATP analogue, the tilt of V₀ changed with respect to V₁, and the stalk region was less clearly defined, perhaps due to increased flexibility and partial detachment of some of the peripheral stalks. These structural changes corresponded to decreased stability of the complex and might be the initial step in a controlled disassembly.

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