Rotary Motor ATPases

  • Stephan WilkensEmail author
Part of the Biophysics for the Life Sciences book series (BIOPHYS, volume 6)


The preceding chapters offered an introduction to a selection of biophysical tools most commonly used in the elucidation of the structure and mechanism of biological macromolecules. The following chapter describes how some of these tools were applied—and new ones developed—to gain an understanding of the catalytic mechanism of a particular class of membrane-bound transport proteins, the rotary motor ATPases. Rotary motor ATPases are highly efficient molecular machines that function to interconvert chemical energy (in form of ATP) into the potential energy of transmembrane ion motive force, and vice versa. Energy conversion in the rotary ATPases involves rotation of a central subdomain (the rotor) relative to a static portion called the stator. Most rotary motor ATPases can function in both directions, which means that the enzyme can either pump ions across lipid membranes at the expense of ATP hydrolysis or synthesize ATP driven by ion flow along a concentration gradient through the membrane-bound part of the complex. Catalysis involving subunit rotation was proposed before detailed structural information was available; however, proving the existence of a rotary mechanism turned out to be a biophysical challenge, and, along the way, novel single molecule observation techniques had to be developed to be able to confirm the rotary motor hypothesis. Rotary motor ATPases can be found in all domains of life including bacteria, archaea, and eukarya. The enzyme found in the inner membrane of mitochondria, the plasma membrane of bacteria, and the thylakoid membrane of chloroplasts is called F1Fo-ATP synthase or F-ATPase. The enzyme found in archaea is called A-ATP synthase (or A1Ao-ATP synthase or A-ATPase) and the enzyme found in the endomembrane system (and sometimes plasma membrane) of eukaryotic organisms is called vacuolar ATPase (or V1Vo-ATPase or V-ATPase). The family of the rotary ATPases is characterized by a similar overall topology, a cytoplasmic ATPase connected to a membrane-bound ion channel, with differences in subunit composition and structure that have evolved to accommodate different functional needs and mechanisms of enzyme regulation.


ATPase Rotary molecular motor F-ATP synthase A-ATP synthase Vacuolar ATPase Biophysics X-ray crystallography Electron microscopy NMR spectroscopy Small angle X-ray scattering Single molecule observation Single molecule fluorescence resonance energy transfer (FRET) spectroscopy 


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© Springer Science+Business Media New York 2013

Authors and Affiliations

  1. 1.Department of Biochemistry and Molecular BiologySUNY Upstate Medical UniversitySyracuseUSA

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