Axle-less F1-ATPase rotates in the correct direction
Axle-less F1-ATPase rotates in the correct direction
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DOI：
10.1126/science.1151343
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发表时间：
2008-02-15
期刊：
影响因子：
56.9
通讯作者：
Kinosita, Kazuhiko, Jr.
中科院分区：
文献类型：
--
作者：
Furuike, Shou;Hossain, Mohammad Delawar;Kinosita, Kazuhiko, Jr.
三磷酸腺苷酶(ATPase)是一种由三磷酸腺苷驱动的旋转分子马达，其中心伽马亚基在由三个α亚基和三个β亚基交替排列的圆柱体内旋转。转动轴是伽马亚基的氨基和羧基末端的反平行阿尔法螺旋线圈，深深地穿透定子圆柱体的中心空腔。我们一步一步地截断轴，直到剩下的转子头在腔外，简单地坐在定子孔的凹口上。所有截断突变体都朝着正确的方向旋转，这意味着扭矩的产生，尽管平均转速较低，较短的突变体表现出不规则的运动时刻。F-1-ATPase的旋转既不需要固定的枢轴，也不需要刚性的轴。
F-1- 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 F-1- ATPase.