Visualizing a new binding site of ncd-motor domain on tubulin

被引:7
作者
Han, Y
Sablin, EP
Nogales, E
Fletterick, RJ
Downing, KH [1 ]
机构
[1] Univ Calif Berkeley, Lawrence Berkeley Lab, Donner Lab, Div Life Sci, Berkeley, CA 94720 USA
[2] Univ Calif San Francisco, Dept Biochem & Biophys, San Francisco, CA 94143 USA
[3] Univ Calif Berkeley, Dept Mol & Cellular Biol, Berkeley, CA 94720 USA
关键词
D O I
10.1006/jsbi.1999.4162
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Ncd is a microtubule minus-end directed motor of the kinesin superfamily. Previously it has been shown that ncd and kinesin motor domains share the same major binding site on microtubules. sere we report a three-dimensional EM reconstruction of negatively stained two-dimensional Zn-induced tubulin crystal sheets (Zn-sheets) decorated with the ncd motor domain at a resolution of 16 Angstrom This work has revealed a second specific binding site for the ncd motor domain. The motor binding site on the tubulin Zn-sheets spans both alpha and beta tubulin subunits. This binding site is located at a position different from the previously identified ncd binding site on microtubules and may play a role in motor function. (C) 1999 Academic Press.
引用
收藏
页码:26 / 33
页数:8
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