Published in
EMBO Press, EMBO Reports, 3(2), p. 229-233, 2001
DOI: 10.1093/embo-reports/kve047
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Bacterial Na+-ATP synthase has an undecameric rotor
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Daniel J. Müller ,
Kitaru Suda,
Dimitrios Fotiadis,
Andreas Engel,
Thomas Meier,
Ulrich Matthey,
Peter Dimroth
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Abstract
Synthesis of adenosine triphosphate (ATP) by the F(1)F(0) ATP synthase involves a membrane-embedded rotary engine, the F(0) domain, which drives the extra-membranous catalytic F(1) domain. The F(0) domain consists of subunits a(1)b(2) and a cylindrical rotor assembled from 9-14 alpha-helical hairpin-shaped c-subunits. According to structural analyses, rotors contain 10 c-subunits in yeast and 14 in chloroplast ATP synthases. We determined the rotor stoichiometry of Ilyobacter tartaricus ATP synthase by atomic force microscopy and cryo-electron microscopy, and show the cylindrical sodium-driven rotor to comprise 11 c-subunits.