期刊
NATURE STRUCTURAL BIOLOGY
卷 10, 期 10, 页码 836-842出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nsb984
关键词
-
To understand the mechanism of kinesin movement we have investigated the relative configuration of the two kinesin motor domains during ATP hydrolysis using fluorescence polarization microscopy of ensemble and single molecules. We found that: ( i) in nucleotide states that induce strong microtubule binding, both motor domains are bound to the microtubule with similar orientations; ( ii) this orientation is maintained during processive motion in the presence of ATP; ( iii) the neck-linker region of the motor domain has distinct configurations for each nucleotide condition tested. Our results fit well with a hand-over-hand type movement mechanism and suggest how the ATPase cycle in the two motor domains is coordinated. We propose that the motor neck-linker domain configuration controls ADP release.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据