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  Structural study on the architecture of the bacterial ATP synthase F0 motor

Hakulinen, J. K., Klyszejko, A. L., Hoffmann, J., Eckardt-Strelau, L., Brutschy, B., Vonck, J., et al. (2012). Structural study on the architecture of the bacterial ATP synthase F0 motor. Proceedings of the National Academy of Sciences of the United States of America, 109(30), E2050-E2056. doi:10.1073/pnas.1203971109.

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 Creators:
Hakulinen, Jonna K.1, Author           
Klyszejko, Adriana L.1, Author           
Hoffmann, Jan2, Author
Eckardt-Strelau, Luise1, Author           
Brutschy, Bernd2, Author
Vonck, Janet1, Author           
Meier, Thomas1, Author           
Affiliations:
1Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068291              
2External Organizations, ou_persistent22              

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Free keywords: bioenergetics; membrane protein complex; 2D crystallization; ion translocation mechanism; membrane Fo rotor-stator
 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.

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Language(s): eng - English
 Dates: 2012-06-262012-07-24
 Publication Status: Published in print
 Pages: 7
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 611350
DOI: 10.1073/pnas.1203971109
 Degree: -

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Title: Proceedings of the National Academy of Sciences of the United States of America
  Other : PNAS
  Other : Proceedings of the National Academy of Sciences of the USA
  Abbreviation : Proc. Natl. Acad. Sci. U. S. A.
Source Genre: Journal
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Affiliations:
Publ. Info: Washington, D.C. : National Academy of Sciences
Pages: - Volume / Issue: 109 (30) Sequence Number: - Start / End Page: E2050 - E2056 Identifier: ISSN: 0027-8424
CoNE: https://pure.mpg.de/cone/journals/resource/954925427230