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

Stahlberg, H. and Müller, D. J. and Suda, K. and Fotiadis, D. and Engel, A. and Meier, T. and Matthey, U. and Dimroth, P.. (2001) Bacterial Na(+)-ATP synthase has an undecameric rotor. EMBO reports, Vol. 2, H. 3. pp. 229-233.

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Official URL: http://edoc.unibas.ch/dok/A5257658

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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.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Structural Biology (Engel)
05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology (Stahlberg)
UniBasel Contributors:Engel, Andreas H and Stahlberg, Henning
Item Type:Article, refereed
Article Subtype:Research Article
Bibsysno:Link to catalogue
Publisher:Nature Publishing Group
ISSN:1469-221X
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:08 Jun 2012 06:44
Deposited On:22 Mar 2012 13:18

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