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Bacterial Na(+)-ATP synthase has an undecameric rotor
Journal
EMBO reports
Volume
2
Number
3
Pages / Article-Number
229-33
Keywords
Bacteria; Anaerobic/enzymology; Cryoelectron Microscopy; Crystallization; Microscopy; Atomic Force; Protein Structure; Tertiary; Protein Subunits; Proton-Translocating ATPases/*chemistry/metabolism/*ultrastructure; Rotation
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.
