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 > Former Organization Units Biozentrum > Structural Biology (Stahlberg) |
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UniBasel Contributors: | Engel, Andreas H and Stahlberg, Henning |
Item Type: | Article, refereed |
Article Subtype: | Research Article |
Publisher: | Nature Publishing Group |
ISSN: | 1469-221X |
Note: | Publication type according to Uni Basel Research Database: Journal article |
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Identification Number: |
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Last Modified: | 08 Jun 2012 06:44 |
Deposited On: | 22 Mar 2012 13:18 |
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