Crossref journal-article
Proceedings of the National Academy of Sciences
Proceedings of the National Academy of Sciences (341)
Abstract

We purified the F o complex from the Ilyobacter tartaricus Na + -translocating F 1 F o -ATP synthase and performed a biochemical and structural study. Laser-induced liquid bead ion desorption MS analysis demonstrates that all three subunits of the isolated F o complex were present and in native stoichiometry (ab 2 c 11 ). Cryoelectron microscopy of 2D crystals yielded a projection map at a resolution of 7.0 Å showing electron densities from the c 11 rotor ring and up to seven adjacent helices. A bundle of four helices belongs to the stator a-subunit and is in contact with c 11 . A fifth helix adjacent to the four-helix bundle interacts very closely with a c-subunit helix, which slightly shifts its position toward the ring center. Atomic force microscopy confirms the presence of the F o stator, and a height profile reveals that it protrudes less from the membrane than c 11 . The data limit the dimensions of the subunit a/c-ring interface: Three helices from the stator region are in contact with three c 11 helices. The location and distances of the stator helices impose spatial restrictions on the bacterial F o complex.

Bibliography

Hakulinen, J. K., Klyszejko, A. L., Hoffmann, J., Eckhardt-Strelau, L., Brutschy, B., Vonck, J., & Meier, T. (2012). Structural study on the architecture of the bacterial ATP synthase F o motor. Proceedings of the National Academy of Sciences, 109(30).

Dates
Type When
Created 13 years, 1 month ago (June 27, 2012, 11:40 a.m.)
Deposited 3 years, 4 months ago (April 12, 2022, 8:48 p.m.)
Indexed 1 year, 1 month ago (July 22, 2024, 3:18 a.m.)
Issued 13 years, 1 month ago (June 26, 2012)
Published 13 years, 1 month ago (June 26, 2012)
Published Online 13 years, 1 month ago (June 26, 2012)
Published Print 13 years ago (July 24, 2012)
Funders 0

None

@article{Hakulinen_2012, title={Structural study on the architecture of the bacterial ATP synthase F o motor}, volume={109}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.1203971109}, DOI={10.1073/pnas.1203971109}, number={30}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Hakulinen, Jonna K. and Klyszejko, Adriana L. and Hoffmann, Jan and Eckhardt-Strelau, Luise and Brutschy, Bernd and Vonck, Janet and Meier, Thomas}, year={2012}, month=jun }