Connecting stalks in V-type ATPase

E.J. Boekema (), J.F.L. van Breemen, A. Brisson, T. Ubbink-Kok, W.N. Konings and J.S. Lolkema
Additional contact information
E.J. Boekema: Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen
J.F.L. van Breemen: Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen
A. Brisson: Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen
T. Ubbink-Kok: Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen
W.N. Konings: Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen
J.S. Lolkema: Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen

Nature, 1999, vol. 401, issue 6748, 37-38

Abstract: 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.

Date: 1999
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DOI: 10.1038/43369

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