Structure insights into mechanisms of ATP hydrolysis and the activation of human heat-shock protein 90
Structure insights into mechanisms of ATP hydrolysis and the activation of human heat-shock protein 90
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ATP 水解机制和人类热休克蛋白激活的结构见解 90
DOI：
10.1093/abbs/gms001
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发表时间：
2012-04-01
影响因子：
3.7
通讯作者：
He, Jianhua
中科院分区：
文献类型：
--
作者：
Li, Jian;Sun, Lihua;He, Jianhua
分子伴侣热休克蛋白90（Hsp 90）的活化依赖于ATP结合和水解，这发生在蛋白质的N端结构域。在这里，我们已经确定了三个晶体结构的N-末端结构域的人热休克蛋白90在天然和与ATP和ATP类似物的复合物，提供了一个清晰的视图ATP水解的催化机制热休克蛋白90。此外，ATP的结合导致N端结构域处于中间状态，这可以部分解释为什么分离的Hsp 90 N端结构域具有非常弱的ATP水解活性。
The activation of molecular chaperone heat-shock protein 90 (Hsp90) is dependent on ATP binding and hydrolysis, which occurs in the N-terminal domains of protein. Here, we have determined three crystal structures of the N-terminal domain of human Hsp90 in native and in complex with ATP and ATP analog, providing a clear view of the catalytic mechanism of ATP hydrolysis by Hsp90. Additionally, the binding of ATP leads the N-terminal domains to be an intermediate state that could be used to partially explain why the isolated N-terminal domain of Hsp90 has very weak ATP hydrolytic activity.