Conformational shift in the closed state of GroEL induced by ATP-binding triggers a transition to the open state.
Conformational shift in the closed state of GroEL induced by ATP-binding triggers a transition to the open state.
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DOI：
10.2142/biophysico.13.0_127
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发表时间：
2016
影响因子：
1.5
通讯作者：
Yura K
中科院分区：
文献类型：
--
作者：
Suzuki Y;Yura K
我们研究了ATP与GroEL结合的效果，并阐明了ATP在GroEL构象变化中的作用。GroEL是一种十四聚体伴侣蛋白，其通过经历从封闭状态到开放状态的构象变化来帮助蛋白质折叠。这种构象变化需要ATP，但不需要ATP的水解。以下三种类型的构象结晶和原子坐标是可用的：封闭状态没有ATP，封闭状态与ATP和开放状态与ADP。我们使用弹性网络模型模拟了从封闭状态到开放状态，以及从封闭状态到开放状态，ATP靶向ATP的构象变化。强调最低正常模式的模拟表明，从含ATP的闭合状态开始的模式，而不是不含ATP的模式，达到了更接近开放状态的构象。这种差异主要是由初始结构中残基位置的变化引起的，而不是亚基内残基“连接性”的变化。我们的研究结果表明，ATP应该表现为绝缘体，诱导构象群体转变的构象，有一个途径，导致开放状态的封闭状态。
We investigated the effect of ATP binding to GroEL and elucidated a role of ATP in the conformational change of GroEL. GroEL is a tetradecamer chaperonin that helps protein folding by undergoing a conformational change from a closed state to an open state. This conformational change requires ATP, but does not require the hydrolysis of the ATP. The following three types of conformations are crystalized and the atomic coordinates are available; closed state without ATP, closed state with ATP and open state with ADP. We conducted simulations of the conformational change using Elastic Network Model from the closed state without ATP targeting at the open state, and from the closed state with ATP targeting at the open state. The simulations emphasizing the lowest normal mode showed that the one started with the closed state with ATP, rather than the one without ATP, reached a conformation closer to the open state. This difference was mainly caused by the changes in the positions of residues in the initial structure rather than the changes in “connectivity” of residues within the subunit. Our results suggest that ATP should behave as an insulator to induce conformation population shift in the closed state to the conformation that has a pathway leading to the open state.