Electron microscopy of the reconstituted complexes of the F1‐ATPase with various subunit constitution revealed the location of the γ subunit in the central cavity of the molecule

FEBS Letters

Wakabayashi, Takeyuki²  Yokoyama, Ken¹  Fujiyama, Yuichiro¹  Yoshida, Masasuke¹ 

[1] Department of Life Science, Tokyo Institute of Technology, Nagatsuta 4259, Midori-ku, Yokohama 227 Japan;Department of Physics, Faculty of Science, University of Tokyo, Bunkyo-ku, Tokyo 113, Japan

关键词: F1-ATPase;    Electron micrograph;    ATPase;    Thermophilic bacterium;    TF1;    F1ATPase from the thermophilic bacterium PS3;   

DOI  :  10.1016/0014-5793(90)80384-U

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The subunit structure of the F₁-ATPase from the thermophilic bacterium PS3 was probed by comparing electron microscopic images of the subunit complexes reconstituted to contain different subunit compositions. The following structural features were observed. (1) The α₃β₃ complex has a hexagonal, apparently symmetrical arrangement of masses with a central cavity. (2) The projections of the α₃β₃δ complexes are similar to those of the α₃β₃ complexes. (3) In contrast, the α₃β₃λ complex has an additional mass in the centre which is similar to that found in the native enzyme (α₃β₃γδϵ). From these observations, it is concluded that the central mass in the F₁-ATPase is comprised mostly of the γ subunit.

【 授权许可】

Unknown