Bovine F1Fo ATP synthase monomers bend the lipid bilayer in 2D membrane crystals

eLife

Yoshinori Fujiyoshi¹  Werner Kühlbrandt²  Kazutoshi Tani²  Karen M Davies³  Deryck J Mills³  Christoph Gerle³  Chimari Jiko⁴  Shintaro Maeda⁵  Kyoko Shinzawa-Itoh⁵  Tomitake Tsukihara⁵ 

[1] Core Research for Evolutional Science and Technology, Japan Science and Technology Agency, Kawaguchi, Japan;Cellular and Structural Physiology Institute, Nagoya University, Nagoya, Japan;Department of Structural Biology, Max Planck Institute of Biophysics, Frankfurt am Main, Germany;Institute for Protein Research, Osaka University, Osaka, Japan;Picobiology Institute, Department of Life Science, Graduate School of Life Science, University of Hyogo, Kamigori, Japan;

关键词: bos taurus;    mitochondria;    membrane curvature;    electron cryo-tomography;    electron crystallography;    sub-tomogram averaging;   

DOI  :  10.7554/eLife.06119

来源: DOAJ

【 摘 要 】

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.

【 授权许可】

Unknown