Structure of the Kinesin13-Microtubule Ring Complex

被引:41
作者
Tan, Dongyan [1 ]
Rice, William J. [2 ]
Sosa, Hernando [1 ]
机构
[1] Albert Einstein Coll Med, Dept Physiol & Biophys, Bronx, NY 10461 USA
[2] New York Struct Biol Ctr, New York, NY 10027 USA
基金
美国国家卫生研究院;
关键词
D O I
10.1016/j.str.2008.08.017
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
To investigate the mechanism of kinesin13-induced microtubule depolymerization, we have calculated a three-dimensional (3D) map of the kinesin13-microtubule ring complex, using cryo-electron microscopy (cryo-EM) and image analysis. An atomic model of the complex was produced by docking the crystal structures of tubulin and a kinesin13 motor domain (MD) into the 3D map. The model reveals a snapshot of the depolymerization mechanism by providing a 3D view of the complex formed between the kinesin13 MD and a curved tubulin protofilament (pf). It suggests that contacts mediated by kinesin13 class-specific residues in the putative microtubule-binding site stabilize intra-dimer tubulin curvature. In addition, a tubulin-binding site on the kinesin13 MD was identified. Mutations at this class-conserved site selectively disrupt the formation of microtubule-associated ring complexes.
引用
收藏
页码:1732 / 1739
页数:8
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