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Biological motors

Connecting stalks in V-type ATPase

Nature volume 401, pages 37–38 (1999)Cite this article

Abstract

In all organisms, adenosine triphosphate (ATP) provides metabolic energy for driving energy-dependent processes. It is synthesized and/or utilized by enzymes known as F-type and V-type ATPases, which are small rotary motors1,2. Both types consist of a headpiece, F1 or V1, respectively, which is connected by a stalk region to the membrane-bound part, FO or VO. Electron microscopic analysis of negatively stained particles has revealed a peripheral stalk, or stator, between V1 and VO of the V-type (Na+)ATPase of the thermophilic bacterium Clostridium fervidus3,4, like that in F-type ATPases5,6. We have analysed many more particles and now present a more complete structure of the V-type ATPase stator moiety.

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Figure 1: Electron microscopy images of V1V0 in side view.

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Author information

Affiliations

  1. Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Groningen, 9747, The Netherlands

    E.J. Boekema, J.F.L. van Breemen, A. Brisson, T. Ubbink-Kok, W.N. Konings & J.S. Lolkema

Authors
  1. E.J. Boekema
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  2. J.F.L. van Breemen
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  3. A. Brisson
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  4. T. Ubbink-Kok
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  5. W.N. Konings
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  6. J.S. Lolkema
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Corresponding author

Correspondence to E.J. Boekema.

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Boekema, E., van Breemen, J., Brisson, A. et al. Connecting stalks in V-type ATPase. Nature 401, 37–38 (1999). https://doi.org/10.1038/43369

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