Bovine F1Fo ATP synthase monomers bend the lipid bilayer in 2D membrane crystals
Chimari Jiko,
Karen M Davies,
Kyoko Shinzawa-Itoh,
Kazutoshi Tani,
Shintaro Maeda,
Deryck J Mills,
Tomitake Tsukihara,
Yoshinori Fujiyoshi,
Werner Kühlbrandt,
Christoph Gerle
Affiliations
Chimari Jiko
Institute for Protein Research, Osaka University, Osaka, Japan
Karen M Davies
Department of Structural Biology, Max Planck Institute of Biophysics, Frankfurt am Main, Germany
Kyoko Shinzawa-Itoh
Picobiology Institute, Department of Life Science, Graduate School of Life Science, University of Hyogo, Kamigori, Japan
Kazutoshi Tani
Cellular and Structural Physiology Institute, Nagoya University, Nagoya, Japan
Shintaro Maeda
Picobiology Institute, Department of Life Science, Graduate School of Life Science, University of Hyogo, Kamigori, Japan
Deryck J Mills
Department of Structural Biology, Max Planck Institute of Biophysics, Frankfurt am Main, Germany
Tomitake Tsukihara
Picobiology Institute, Department of Life Science, Graduate School of Life Science, University of Hyogo, Kamigori, Japan; Core Research for Evolutional Science and Technology, Japan Science and Technology Agency, Kawaguchi, Japan
Yoshinori Fujiyoshi
Cellular and Structural Physiology Institute, Nagoya University, Nagoya, Japan
Werner Kühlbrandt
Department of Structural Biology, Max Planck Institute of Biophysics, Frankfurt am Main, Germany
Picobiology Institute, Department of Life Science, Graduate School of Life Science, University of Hyogo, Kamigori, Japan; Core Research for Evolutional Science and Technology, Japan Science and Technology Agency, Kawaguchi, Japan
We have used a combination of electron cryo-tomography, subtomogram averaging, and electron crystallographic image processing to analyse the structure of intact bovine F1Fo ATP synthase in 2D membrane crystals. ATPase assays and mass spectrometry analysis of the 2D crystals confirmed that the enzyme complex was complete and active. The structure of the matrix-exposed region was determined at 24 Å resolution by subtomogram averaging and repositioned into the tomographic volume to reveal the crystal packing. F1Fo ATP synthase complexes are inclined by 16° relative to the crystal plane, resulting in a zigzag topology of the membrane and indicating that monomeric bovine heart F1Fo ATP synthase by itself is sufficient to deform lipid bilayers. This local membrane curvature is likely to be instrumental in the formation of ATP synthase dimers and dimer rows, and thus for the shaping of mitochondrial cristae.
