The crystal structure of the nucleotide-free alpha 3 beta 3 subcomplex of F-1-ATPase from the thermophilic Bacillus PS3 is a symmetric trimer

Shirakihara, Yasuo and Leslie, Andrew G. W. and Abrahams, Jan Pieter and Walker, John E. and Ueda, Takashi and Sekimoto, Yoshinori and Kambara, Minoru and Saika, Kouji and Kagawa, Yasuo and Yoshida, Masasuke. (1997) The crystal structure of the nucleotide-free alpha 3 beta 3 subcomplex of F-1-ATPase from the thermophilic Bacillus PS3 is a symmetric trimer. Structure, 5 (6). pp. 825-836.

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Background: F-1-ATPase, an oligomeric assembly with subunit stoichiometry alpha 3 beta 3 gamma delta epsilon, is the catalytic component of the ATP synthase complex, which plays a central role in energy transduction in bacteria, chloroplasts and mitochondria. The crystal structure of bovine mitochondrial F-1-ATPase displays a marked asymmetry in the conformation and nucleotide content of the catalytic beta subunits, The alpha 3 beta 3 subcomplex of F-1-ATPase has been assembled from subunits of the moderately thermophilic Bacillus PS3 made in Escherichia coli, and the subcomplex is active but does not show the catalytic cooperativity of intact F-1-ATPase. The structure of this subcomplex should provide new information on the conformational variability of F-1-ATPase and may provide insights into the unusual catalytic mechanism employed by this enzyme.Results: The crystal structure of the nucleotide-free bacterial alpha 3 beta 3 subcomplex of F-1-ATPase, determined at 3.2 Angstrom resolution, shows that the oligomer has exact threefold symmetry. The bacterial beta subunits adopt a conformation essentially identical to that of the nucleotide-free beta subunit in mitochondrial F-1-ATPase; the alpha subunits have similar conformations in both structures.Conclusions: The structures of the bacterial F-1-ATPase alpha and beta subunits are very similar to their counterparts in the mitochondrial enzyme, suggesting a common catalytic mechanism. The study presented here allows an analysis of the different conformations adopted by the alpha and beta subunits and may ultimately further our understanding of this mechanism.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Nano-diffraction of Biological Specimen (Abrahams)
UniBasel Contributors:Abrahams, Jan Pieter
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:Cell Press
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:05 Nov 2020 14:51
Deposited On:05 Nov 2020 14:51

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