ArticleProceedings of the National Academy of Sciences of the United States of America2012
Structural study on the architecture of the bacterial ATP synthase Fo motor.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Purification and Reconstitution of Ilyobacter tartaricus ATP Synthase.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Article
- Mouse-to-mouse variation in maturation heterogeneity of smooth muscle cells.Lab on a chip · 2018Article
- Horizontal membrane-intrinsic α-helices in the stator a-subunit of an F-type ATP synthase.Nature · 2015Article
- Structure of the mycobacterial ATP synthase Fo rotor ring in complex with the anti-TB drug bedaquiline.Science advances · 2015Article
- Fo-driven Rotation in the ATP Synthase Direction against the Force of F1 ATPase in the FoF1 ATP Synthase.The Journal of biological chemistry · 2015Article
- Interacting cytoplasmic loops of subunits a and c of Escherichia coli F1F0 ATP synthase gate H+ transport to the cytoplasm.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Obstruction of transmembrane helical movements in subunit a blocks proton pumping by F1Fo ATP synthase.The Journal of biological chemistry · 2013Article
- Interactions between subunits a and b in the rotary ATP synthase as determined by cross-linking.FEBS letters · 2013Article
- Twisting and subunit rotation in single F(O)(F1)-ATP synthase.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2013Review
- Resolving the negative potential side (n-side) water-accessible proton pathway of F-type ATP synthase by molecular dynamics simulations.The Journal of biological chemistry · 2012Article
- Review
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
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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