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- Title
Bacterial Na<sup>+</sup>-ATP synthase has an undecameric rotor.
- Authors
Stahlberg, Henning; Müller, Daniel J.; Suda, Kitaru; Fotiadis, Dimitrios; Engel, Andreas; Meier, Thomas; Matthey, Ulrich; Dimroth, Peter
- Abstract
Synthesis of adenosine triphosphate (ATP) by the F1F0 ATP synthase involves a membrane-embedded rotary engine, the F0 domain, which drives the extra-membranous catalytic F1 domain. The F0 domain consists of subunits a1b2 and a cylindrical rotor assembled from 9-14 α-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.
- Subjects
ENZYMES; ADENOSINE triphosphatase; WANKEL engine; CHLOROPLASTS; YEAST; STOICHIOMETRY
- Publication
EMBO Reports, 2001, Vol 2, Issue 3, p229
- ISSN
1469-221X
- Publication type
Report
- DOI
10.1093/embo-reports/kve047