A Distinct Meta-active Conformation in the 1.1-Å Resolution Structure of Wild-type ApoCheY*

A Distinct Meta-active Conformation in the 1.1-Å Resolution Structure of Wild-type ApoCheY*
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野生型 ApoCheY* 1.1-Å 分辨率结构中独特的元活性构象

DOI:
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发表时间:
2001
影响因子:
4.8
通讯作者:
K. Volz
K. Volz
中科院分区:
生物学2区
文献类型:
--
作者:
M. Simonović;K. Volz

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CheY是反应调节因子超家族中最具特征的成员,因此它已成为理解双组分系统中信号传导的初始分子机制的主要模型。反应调节因子的正常信号传导需要磷酸化,结合其构象效应尚未完全理解的激活机制。CheY的激活涉及三个事件:磷酸化、β4-α 4环的构象变化和酪氨酸106侧链的旋转限制。一个悬而未决的问题是apoCheY群体中活性构象的性质。野生型apoCheY的1.08-nm分辨率晶体结构的细节显示了两种明显不同构象的β4-α4环,其与酪氨酸106侧链的两个旋转异构体位置空间相关。CheY的这些构象状态之一是非活性形式,我们建议另一种是亚活性形式,负责apoCheY中看到的活性特性。
CheY is the best characterized member of the response regulator superfamily, and as such it has become the principal model for understanding the initial molecular mechanisms of signaling in two-component systems. Normal signaling by response regulators requires phosphorylation, in combination with an activation mechanism whose conformational effects are not completely understood. CheY activation involves three events, phosphorylation, a conformational change in the β4–α4loop, and a rotational restriction of the side chain of tyrosine 106. An outstanding question concerns the nature of an active conformation in the apoCheY population. The details of this 1.08-Å resolution crystal structure of wild-type apoCheY shows the β4–α4 loop in two distinctly different conformations that sterically correlate with the two rotameric positions of the tyrosine 106 side chain. One of these conformational states of CheY is the inactive form, and we propose that the other is a meta-active form, responsible for the active properties seen in apoCheY.
DOI: 10.1016/s0021-9258(18)92982-0
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