Bovine F1Fo ATP synthase monomers bend the lipid bilayer in 2D membrane crystals
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...
| Main Authors: | , , , , , , , , , |
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| Format: | Article |
| Language: | English |
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eLife Sciences Publications Ltd
2015-03-01
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| Series: | eLife |
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| Online Access: | https://elifesciences.org/articles/06119 |
| _version_ | 1811200399641673728 |
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| author | Chimari Jiko Karen M Davies Kyoko Shinzawa-Itoh Kazutoshi Tani Shintaro Maeda Deryck J Mills Tomitake Tsukihara Yoshinori Fujiyoshi Werner Kühlbrandt Christoph Gerle |
| author_facet | Chimari Jiko Karen M Davies Kyoko Shinzawa-Itoh Kazutoshi Tani Shintaro Maeda Deryck J Mills Tomitake Tsukihara Yoshinori Fujiyoshi Werner Kühlbrandt Christoph Gerle |
| author_sort | Chimari Jiko |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-04-12T02:02:47Z |
| format | Article |
| id | doaj.art-c8beb6e1106b4cb8bab9a8fa0ea205a2 |
| institution | Directory Open Access Journal |
| issn | 2050-084X |
| language | English |
| last_indexed | 2024-04-12T02:02:47Z |
| publishDate | 2015-03-01 |
| publisher | eLife Sciences Publications Ltd |
| record_format | Article |
| series | eLife |
| spelling | doaj.art-c8beb6e1106b4cb8bab9a8fa0ea205a22022-12-22T03:52:37ZengeLife Sciences Publications LtdeLife2050-084X2015-03-01410.7554/eLife.06119Bovine F1Fo ATP synthase monomers bend the lipid bilayer in 2D membrane crystalsChimari Jiko0Karen M Davies1Kyoko Shinzawa-Itoh2Kazutoshi Tani3Shintaro Maeda4Deryck J Mills5Tomitake Tsukihara6Yoshinori Fujiyoshi7Werner Kühlbrandt8Christoph Gerle9https://orcid.org/0000-0002-7265-2804Institute for Protein Research, Osaka University, Osaka, JapanDepartment of Structural Biology, Max Planck Institute of Biophysics, Frankfurt am Main, GermanyPicobiology Institute, Department of Life Science, Graduate School of Life Science, University of Hyogo, Kamigori, JapanCellular and Structural Physiology Institute, Nagoya University, Nagoya, JapanPicobiology Institute, Department of Life Science, Graduate School of Life Science, University of Hyogo, Kamigori, JapanDepartment of Structural Biology, Max Planck Institute of Biophysics, Frankfurt am Main, GermanyPicobiology 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, JapanCellular and Structural Physiology Institute, Nagoya University, Nagoya, JapanDepartment of Structural Biology, Max Planck Institute of Biophysics, Frankfurt am Main, GermanyPicobiology 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, JapanWe 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.https://elifesciences.org/articles/06119bos taurusmitochondriamembrane curvatureelectron cryo-tomographyelectron crystallographysub-tomogram averaging |
| spellingShingle | Chimari Jiko Karen M Davies Kyoko Shinzawa-Itoh Kazutoshi Tani Shintaro Maeda Deryck J Mills Tomitake Tsukihara Yoshinori Fujiyoshi Werner Kühlbrandt Christoph Gerle Bovine F1Fo ATP synthase monomers bend the lipid bilayer in 2D membrane crystals eLife bos taurus mitochondria membrane curvature electron cryo-tomography electron crystallography sub-tomogram averaging |
| title | Bovine F1Fo ATP synthase monomers bend the lipid bilayer in 2D membrane crystals |
| title_full | Bovine F1Fo ATP synthase monomers bend the lipid bilayer in 2D membrane crystals |
| title_fullStr | Bovine F1Fo ATP synthase monomers bend the lipid bilayer in 2D membrane crystals |
| title_full_unstemmed | Bovine F1Fo ATP synthase monomers bend the lipid bilayer in 2D membrane crystals |
| title_short | Bovine F1Fo ATP synthase monomers bend the lipid bilayer in 2D membrane crystals |
| title_sort | bovine f1fo atp synthase monomers bend the lipid bilayer in 2d membrane crystals |
| topic | bos taurus mitochondria membrane curvature electron cryo-tomography electron crystallography sub-tomogram averaging |
| url | https://elifesciences.org/articles/06119 |
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