• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Cell discovery. >Structural basis for Sfm1 functioning as a protein arginine methyltransferase
【24h】

Structural basis for Sfm1 functioning as a protein arginine methyltransferase

机译：Sfm1充当蛋白质精氨酸甲基转移酶的结构基础

获取原文
       
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

SPOUT proteins constitute one class of methyltransferases, which so far are found to exert activity mainly towards RNAs. Previously, yeast Sfm1 was predicted to contain a SPOUT domain but can methylate ribosomal protein S3. Here we report the crystal structure of Sfm1, which comprises of a typical SPOUT domain and a small C-terminal domain. The active site is similar to that of protein arginine methyltransferases but different from that of RNA methyltransferases. In addition, Sfm1 exhibits a negatively charged surface surrounding the active site unsuitable for RNA binding. Our biochemical data show that Sfm1 exists as a monomer and has high activity towards ribosomal protein S3 but no activity towards RNA. It can specifically catalyze the methylation of Arg146 of S3 and the C-terminal domain is critical for substrate binding and activity. These results together provide the structural basis for Sfm1 functioning as a PRMT for ribosomal protein S3.
机译：SPOUT蛋白构成了一类甲基转移酶，到目前为止，发现它们主要对RNA发挥活性。以前，酵母Sfm1预计含有SPOUT结构域，但可以使核糖体蛋白S3甲基化。在这里，我们报告Sfm1的晶体结构，其中包括一个典型的SPOUT域和一个小的C端域。活性位点类似于蛋白质精氨酸甲基转移酶，但不同于RNA甲基转移酶。此外，Sfm1在围绕活性位点的负电荷表面不适合RNA结合。我们的生化数据表明，Sfm1作为单体存在，对核糖体蛋白S3具有高活性，但对RNA无活性。它可以特异性催化S3的Arg146的甲基化，而C末端结构域对于底物结合和活性至关重要。这些结果共同为Sfm1充当核糖体蛋白S3的PRMT发挥了结构基础。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号