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The Journal of Experimental Biology 204, 2597-2605 (2001)
© 2001 The Company of Biologists Limited

Review

Structure–function relationships of A-, F- and V-ATPases

Gerhard Grüber^1,*, Helmut Wieczorek², William R. Harvey³ and Volker Müller⁴

¹ FR 2.5 Biophysik, Universität des Saarlandes, D-66421 Homburg, Germany,
² Department of Biology, University of Osnabrück, D-49069 Osnabrück, Germany,
³ Whitney Laboratory, University of Florida, St Augustine, FL 32080, USA and
⁴ Lehrstuhl für Mikrobiologie der Ludwig-Maximilians-Universität München, D-80638, München, Germany

*Author for correspondence (e-mail: ggrueber{at}med-rz.uni-saarland.de)

Accepted May 9, 2001

Ion-translocating ATPases, such as the F₁F_o-, V₁V_o- and archaeal A₁A_o enzymes, are essential cellular energy converters which transduce the chemical energy of ATP hydrolysis into transmembrane ionic electrochemical potential differences. Based on subunit composition and primary structures of the subunits, these types of ATPases are related through evolution; however, they differ with respect to function. Recent work has focused on the three-dimensional structural relationships of the major, nucleotide-binding subunits A and B of the A₁/V₁-ATPases and the corresponding ß and subunits of the F₁-ATPase, and the location of the coupling subunits within the stalk that provide the physical linkage between the regions of ATP hydrolysis and ion transduction. This review focuses on the structural homologies and diversities of A₁-, F₁- and V₁-ATPases, in particular on significant differences between the stalk regions of these families of enzymes.

Key words: A₁A_o-ATPase, archaea-type ATPase, F₁F_o-ATPase, H⁺ translocating vacuolar-type ATPase, V₁-ATPase, small-angle X-ray scattering, Escherichia coli, Manduca sexta, Methanosarcina mazei.

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