抗病毒蛋白 viperin 是一种自由基 SAM 酶。
The antiviral protein viperin is a radical SAM enzyme.
机构信息
Department of Chemistry and Biochemistry, Montana State University, Bozeman, MT 59717, USA.
出版信息
FEBS Lett. 2010 Mar 19;584(6):1263-7. doi: 10.1016/j.febslet.2010.02.041. Epub 2010 Feb 20.
Abstract
Viperin, an interferon-inducible antiviral protein, is shown to bind an iron-sulfur cluster, based on iron analysis as well as UV-Vis and electron paramagnetic resonance spectroscopic data. The reduced protein contains a 4Fe-4S cluster whose g-values are altered upon addition of S-adenosylmethionine (SAM), consistent with SAM coordination to the cluster. Incubation of reduced viperin with SAM results in reductive cleavage of SAM to produce 5'-deoxyadenosine (5'-dAdo), a reaction characteristic of the radical SAM superfamily. The 5'-dAdo cleavage product was identified by a combination of HPLC and mass spectrometry analysis.
摘要
Viperin，一种干扰素诱导的抗病毒蛋白，被证明可以结合铁硫簇，这是基于铁分析以及紫外可见和电子顺磁共振波谱数据得出的结论。还原后的蛋白含有一个4Fe-4S簇，其 g 值在添加 S-腺苷甲硫氨酸（SAM）后发生改变，这与 SAM 与簇的配位一致。还原型 viperin 与 SAM 孵育会导致 SAM 的还原裂解，产生 5'-脱氧腺苷（5'-dAdo），这是自由基 SAM 超家族的特征反应。通过 HPLC 和质谱分析的组合，鉴定了 5'-dAdo 裂解产物。
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