research article
Bacterial Na+-ATP synthase has an undecameric rotor
March 1, 2001
Synthesis of adenosine triphosphate (ATP) by the F1F0 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.
Type
research article
Author(s)
Date Issued
2001-03-01
Publisher
Published in
Volume
2
Issue
3
Start page
229
End page
233
Editorial or Peer reviewed
REVIEWED
Written at
OTHER
EPFL units
Available on Infoscience
February 13, 2020
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