Bacterial Na(+)-ATP synthase has an undecameric rotor.
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.
M.E. Müller Institute for Structural Biology, Biozentrum, University of Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland.
H
H
Stahlberg
D J
DJ
Müller
K
K
Suda
D
D
Fotiadis
A
A
Engel
T
T
Meier
U
U
Matthey
P
P
Dimroth
D001421:Bacteria, Anaerobic / Q000201:enzymology; D020285:Cryoelectron Microscopy; D003460:Crystallization; D018625:Microscopy, Atomic Force; D017434:Protein Structure, Tertiary; D021122:Protein Subunits; D006180:Proton-Translocating ATPases / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure*; D012399:Rotation
D021122:Protein Subunits; D006180:Proton-Translocating ATPases