Furuike Shou, Hossain Mohammad Delawar, Maki Yasushi, Adachi Kengo, Suzuki Toshiharu, Kohori Ayako, Itoh Hiroyasu, Yoshida Masasuke, Kinosita Kazuhiko
Department of Physics, Faculty of Science and Engineering, Waseda University, Shinjuku-ku, Tokyo 169-8555, Japan.
Science. 2008 Feb 15;319(5865):955-8. doi: 10.1126/science.1151343.
F1-adenosine triphosphatase (ATPase) is an ATP-driven rotary molecular motor in which the central gamma subunit rotates inside a cylinder made of three alpha and three beta subunits alternately arranged. The rotor shaft, an antiparallel alpha-helical coiled coil of the amino and carboxyl termini of the gamma 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.
F1 - 腺苷三磷酸酶（ATP酶）是一种由ATP驱动的旋转分子马达，其中央γ亚基在由三个α亚基和三个β亚基交替排列组成的圆柱体内部旋转。转子轴是γ亚基氨基和羧基末端的反平行α - 螺旋卷曲螺旋，深深穿透定子圆柱体的中心腔。我们逐步截断轴，直到剩余的转子头部位于腔体外，仅位于定子孔的凹形入口上。所有截断突变体均沿正确方向旋转，这意味着产生了扭矩，尽管平均旋转速度较低，且短突变体表现出不规则运动的时刻。F1 - ATP酶的旋转既不需要固定的支点也不需要刚性轴。
