DOI: 10.7554/elife.06119. Bovine F1Fo ATP synthase monomers bend the lipid bilayer in 2D membrane crystals

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

10.7554/elife.06119

Crossref journal-article

eLife Sciences Publications, Ltd

eLife (4374)

Abstract

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.

Bibliography

Jiko, C., Davies, K. M., Shinzawa-Itoh, K., Tani, K., Maeda, S., Mills, D. J., Tsukihara, T., Fujiyoshi, Y., KÃ¼hlbrandt, W., & Gerle, C. (2015). Bovine F1Fo ATP synthase monomers bend the lipid bilayer in 2D membrane crystals. ELife, 4. CLOCKSS.

Authors 10

Chimari Jiko (first)
Karen M Davies (additional)
Kyoko Shinzawa-Itoh (additional)
Kazutoshi Tani (additional)
Shintaro Maeda (additional)
Deryck J Mills (additional)
Tomitake Tsukihara (additional)
Yoshinori Fujiyoshi (additional)
Werner Kühlbrandt (additional)
Christoph Gerle (additional)

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Dates

Type	When
Created	10 years, 4 months ago (March 27, 2015, 5:11 p.m.)
Deposited	1 year, 10 months ago (Oct. 11, 2023, 8:46 p.m.)
Indexed	3 weeks, 2 days ago (July 30, 2025, 1:07 p.m.)
Issued	10 years, 4 months ago (March 27, 2015)
Published	10 years, 4 months ago (March 27, 2015)
Published Online	10 years, 4 months ago (March 27, 2015)

Funders 10

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gov (National government)
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BibTeX

@article{Jiko_2015, title={Bovine F1Fo ATP synthase monomers bend the lipid bilayer in 2D membrane crystals}, volume={4}, ISSN={2050-084X}, url={http://dx.doi.org/10.7554/elife.06119}, DOI={10.7554/elife.06119}, journal={eLife}, publisher={eLife Sciences Publications, Ltd}, author={Jiko, Chimari and Davies, Karen M and Shinzawa-Itoh, Kyoko and Tani, Kazutoshi and Maeda, Shintaro and Mills, Deryck J and Tsukihara, Tomitake and Fujiyoshi, Yoshinori and Kühlbrandt, Werner and Gerle, Christoph}, year={2015}, month=mar }

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  "abstract": "<jats:p>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 \u00c5 resolution by subtomogram averaging and repositioned into the tomographic volume to reveal the crystal packing. F1Fo ATP synthase complexes are inclined by 16\u00b0 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.</jats:p>",
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