Axle-less F1-ATPase rotates in the correct direction

Shou Furuike, Mohammad Delawar Hossain, Yasushi Maki, Kengo Adachi, Toshiharu Suzuki, Ayako Kohori, Hiroyasu Itoh, Masasuke Yoshida, Kazuhiko Kinosita*

*Corresponding author for this work

    Research output: Contribution to journalArticlepeer-review

    92 Citations (Scopus)


    F1-adenosine triphosphatase (ATPase) is an ATP-driven rotary molecular motor in which the central γ subunit rotates inside a cylinder made of three α and three β subunits alternately arranged. The rotor shaft, an antiparallel α-helical coiled coil of the amino and carboxyl termini of the γ subunit, deeply penetrates the central cavity of the stator cylinder. We truncated the shaft step by step until the remaining rotor head would be outside the cavity and simply sat on the concave entrance of the stator orifice. All truncation mutants rotated in the correct direction, implying torque generation, although the average rotary speeds were low and short mutants exhibited moments of irregular motion. Neither a fixed pivot nor a rigid axle was needed for rotation of F1-ATPase.

    Original languageEnglish
    Pages (from-to)955-958
    Number of pages4
    Issue number5865
    Publication statusPublished - 2008 Feb 15

    ASJC Scopus subject areas

    • General
    • Medicine(all)


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