ATP synthase : constrained stoichiometry of the transmembrane rotor

Müller, D. J. and Dencher, N. A. and Meier, T. and Dimroth, P. and Suda, K. and Stahlberg, H. and Engel, A. and Seelert, H. and Matthey, U.. (2001) ATP synthase : constrained stoichiometry of the transmembrane rotor. FEBS letters, Vol. 504, H. 3. pp. 219-222.

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Official URL: http://edoc.unibas.ch/dok/A5262380

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Recent structural data suggest that the number of identical subunits (c or III) assembled into the cation-powered rotor of F(1)F(0) ATP synthase depends on the biological origin. Atomic force microscopy allowed individual subunits of the cylindrical transmembrane rotors from spinach chloroplast and from Ilyobacter tartaricus ATP synthase to be directly visualized in their native-like environment. Occasionally, individual rotors exhibit structural gaps of the size of one or more subunits. Complete rotors and arch-shaped fragments of incomplete rotors revealed the same diameter within one ATP synthase species. These results suggest the rotor diameter and stoichiometry to be determined by the shape of the subunits and their nearest neighbor interactions.
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
Publisher:Elsevier Science
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 13:23

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