X-ray crystal structure of the yeast Kar3 motor domain complexed with Mg•ADP to 2.3 Å resolution
X-ray crystal structure of the yeast Kar3 motor domain complexed with Mg•ADP to 2.3 Å resolution
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DOI：
10.1021/bi972504o
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发表时间：
1998-02-17
期刊：
影响因子：
2.9
通讯作者：
Rayment, I
中科院分区：
文献类型：
--
作者：
Gulick, AM;Song, H;Rayment, I
运动蛋白激酶家族包含一个保守的运动结构域，大约有350个氨基酸，产生针对微管的运动。这个家族的90多个成员已经被确定，包括向微管的负端或正端移动的马达。来自酿酒酵母菌的Kar3蛋白是负端定向运动蛋白家族成员，参与核融合或核分裂。Kar3蛋白全长729个残基，马达结构域位于c端347个残基。最近，两个激酶家族成员的三维结构被报道。这些结构包括正端定向运动蛋白重链的运动域[Kull， F. J., et al. (1996) Nature 380, 550-555]和负端定向Ncd [Sablin， E， P., et al. (1996) Nature 380, 555-559]。我们现在报道了Kar3蛋白与Mg ADP络合的结构，从2.3埃的晶体学数据中得到。该结构与早期的激酶家族成员相似，但也显示出差异，最明显的是在螺旋α 4的长度上，该螺旋被认为参与了水解周期中的构象变化。
The kinesin family of motor proteins, which contain a conserved motor domain of similar to 350 amino acids, generate movement against microtubules. Over 90 members of this family have been identified, including motors that move toward the minus or plus end of microtubules. The Kar3 protein from Saccharomyces cerevisiae is a minus end-directed kinesin family member that is involved in both nuclear fusion, or karyogamy, and mitosis. The Kar3 protein is 729 residues in length with the motor domain located in the C-terminal 347 residues. Recently, the three-dimensional structures of two kinesin family members have been reported. These structures include the motor domains of the plus end-directed kinesin heavy chain [Kull, F. J., et al. (1996) Nature 380, 550-555] and the minus end-directed Ncd [Sablin, E, P., et al. (1996) Nature 380, 555-559]. We now report the structure of the Kar3 protein complexed with Mg ADP obtained from crystallographic data to 2.3 Angstrom. The structure is similar to those of the earlier kinesin family members, but shows differences as well, most notably in the length of helix alpha 4, a helix which is believed to be involved in conformational changes during the hydrolysis cycle.