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Structural biology

Proton-powered turbine of a plant motor

Abstract

ATP synthases are enzymes that can work in two directions to catalyse either the synthesis or breakdown of ATP, and they constitute the smallest rotary motors in biology. The flow of protons propels the rotation1 of a membrane-spanning complex of identical protein subunits, the number of which determines the efficiency of energy conversion. This proton-powered turbine is predicted to consist of 12 subunits2,3,4, based on data for Escherichia coli5. The yeast mitochondrial enzyme, however, has only 10 subunits6. We have imaged the ATP synthase from leaf chloroplasts by using atomic force microscopy and, surprisingly, find that its turbine has 14 subunits, arranged in a cylindrical ring.

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Figure 1: Characterization of subunit-III oligomers.
Figure 2: Subunit-III oligomers of chloroplast ATP synthase visualized in 25 mM MgCl2, 10 mM Tris–HCl, pH 7.8, at room temperature using atomic force microscopy (Nanoscope III, Digital Instruments)11.

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Correspondence to Norbert A. Dencher.

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Seelert, H., Poetsch, A., Dencher, N. et al. Proton-powered turbine of a plant motor . Nature 405, 418–419 (2000). https://doi.org/10.1038/35013148

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