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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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Datensatz-Permalink: https://hdl.handle.net/11858/00-001M-0000-0024-D5A0-D Versions-Permalink: https://hdl.handle.net/21.11116/0000-000C-D277-1
Genre: Zeitschriftenartikel

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

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Schlagwörter: bioenergetics; membrane protein complex; 2D crystallization; ion translocation mechanism; membrane Fo rotor-stator
 Zusammenfassung: 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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Sprache(n): eng - English
 Datum: 2012-06-262012-07-24
 Publikationsstatus: Erschienen
 Seiten: 7
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: eDoc: 611350
DOI: 10.1073/pnas.1203971109
 Art des Abschluß: -

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Titel: Proceedings of the National Academy of Sciences of the United States of America
  Andere : PNAS
  Andere : Proceedings of the National Academy of Sciences of the USA
  Kurztitel : Proc. Natl. Acad. Sci. U. S. A.
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: Washington, D.C. : National Academy of Sciences
Seiten: - Band / Heft: 109 (30) Artikelnummer: - Start- / Endseite: E2050 - E2056 Identifikator: ISSN: 0027-8424
CoNE: https://pure.mpg.de/cone/journals/resource/954925427230