S-Nitrosylation Induces Structural and Dynamical Changes in a Rhodanese Family Protein.
S-Nitrosylation Induces Structural and Dynamical Changes in a Rhodanese Family Protein.
复制标题
S-亚硝基化诱导罗丹家族蛋白的结构和动态变化。
DOI：
10.1016/j.jmb.2016.07.010
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发表时间：
2016-09-25
影响因子：
5.6
通讯作者：
Riek R
中科院分区：
文献类型：
--
作者：
Eichmann C;Tzitzilonis C;Nakamura T;Kwiatkowski W;Maslennikov I;Choe S;Lipton SA;Riek R
S-亚硝基化是蛋白质功能和信号转导中重要的翻译后调节因子。然而，人们对其结构和动态后果知之甚少。我们研究了S-亚硝基化对大肠杆菌整合膜蛋白YgaP的罗丹酸结构域的影响，通过NMR，X-射线晶体学和质谱。结果表明，活性半胱氨酸的Rhodanese结构域的YgaP进行两个竞争性的修改：S-亚硝基化和S-巯基化，这是自然发生在体内。已经观察到，除了抑制硫转移活性之外，活性位点残基Cys63的S-亚硝基化由于活性位点和螺旋偶极之间的相互作用的减弱而导致螺旋5的慢运动和位移的增加。这些发现为亚硝化应激如何在原子水平上发挥作用提供了一个例子。
S-Nitrosylation is well established as an important post-translational regulator in protein function and signaling. However, relatively little is known about its structural and dynamical consequences. We have investigated the effects of S-nitrosylation on the rhodanese domain of the Escherichia coli integral membrane protein YgaP by NMR, X-ray crystallography, and mass spectrometry. The results show that the active cysteine in the rhodanese domain of YgaP is subjected to two competing modifications: S-nitrosylation and S-sulfhydration, which are naturally occurring in vivo. It has been observed that in addition to inhibition of the sulfur transfer activity, S-nitrosylation of the active site residue Cys63 causes an increase in slow motion and a displacement of helix 5 due to a weakening of the interaction between the active site and the helix dipole. These findings provide an example of how nitrosative stress can exert action at the atomic level.