Abstract
The structure of the dimeric ATP synthase from yeast mitochondria was analyzed by transmission electron microscopy and single particle image analysis. In addition to the previously reported side views of the dimer, top view and intermediate projections served to resolve the arrangement of the rotary c(10) ring and the other stator subunits at the F(0)-F(0) dimeric interface. A three-dimensional reconstruction of the complex was calculated from a data set of 9960 molecular images at a resolution of 27 Å. The structural model of the dimeric ATP synthase shows the two monomers arranged at an angle of ∼45°, consistent with our earlier analysis of the ATP synthase from bovine heart mitochondria (Minauro-Sanmiguel, F., Wilkens, S., and Garcia, J. J. (2005) Proc. Natl. Acad. Sci. U.S.A. 102, 12356-12358). In the ATP synthase dimer, the two peripheral stalks are located near the F(1)-F(1) interface but are turned away from each other so that they are not in contact. Based on the three-dimensional reconstruction, a model of how dimeric ATP synthase assembles to form the higher order oligomeric structures that are required for mitochondrial cristae biogenesis is discussed.
Highlights
Subunit in the ATP synthase of Paracoccus denitrificans and related ␣-proteobacteria [8]
The larger angle of the Polytomella enzyme is stabilized by additional subunits not present in yeast and animal ATP synthases, and this enzyme contains nine different proteins named ASA1 to ASA9 instead of the classical subunits that form the peripheral stalk as well as those involved in the dimerization of all other mitochondrial ATP synthases described [31, 32]
Based on the three-dimensional model of dimeric ATP synthase, we suggest that according to previous proposals [24, 25] oligomer formation occurs by packing dimers together with an offset so as to bring the peripheral stalks of two adjacent dimers into contact, consistent with available cross-linking data [11,12,13,14,15, 19, 40]
Summary
Subunit in the ATP synthase of Paracoccus denitrificans and related ␣-proteobacteria [8]. We obtained two-dimensional projections of the yeast mitochondrial ATP synthase dimer that allowed the calculation of a three-dimensional structural model of the complex at a resolution of 27 Å (0.5 FSC; 21 Å using the 3 criterion, see supplemental Fig. S3).
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