Bacterial Na(+)-ATP synthase has an undecameric rotor

H Stahlberg; D J Müller; K Suda; D Fotiadis; A Engel; T Meier; U Matthey; P Dimroth

doi:10.1093/embo-reports/kve047

Bacterial Na(+)-ATP synthase has an undecameric rotor

EMBO Rep. 2001 Mar;2(3):229-33. doi: 10.1093/embo-reports/kve047.

Authors

H Stahlberg¹, D J Müller, K Suda, D Fotiadis, A Engel, T Meier, U Matthey, P Dimroth

Affiliation

¹ M.E. Müller Institute for Structural Biology, Biozentrum, University of Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland.

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Bacteria, Anaerobic / enzymology
Cryoelectron Microscopy
Crystallization
Microscopy, Atomic Force
Protein Structure, Tertiary
Protein Subunits
Proton-Translocating ATPases / chemistry*
Proton-Translocating ATPases / metabolism
Proton-Translocating ATPases / ultrastructure*
Rotation

Substances

Protein Subunits
Proton-Translocating ATPases