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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Structural insight into arginine methylation by the mouse protein arginine methyltransferase 7: a zinc finger freezes the mimic of the dimeric state into a single active site
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Structural insight into arginine methylation by the mouse protein arginine methyltransferase 7: a zinc finger freezes the mimic of the dimeric state into a single active site

机译：结构了解精氨酸甲基化鼠标蛋白质精氨酸甲基转移酶7:a锌指二聚的的模拟结冰成一个单一的活性部位

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摘要

Protein arginine methyltransferase 7 (PRMT7) is a type III arginine methyltransferase which has been implicated in several biological processes such as transcriptional regulation, DNA damage repair, RNA splicing, cell differentiation and metastasis. PRMT7 is a unique but less characterized member of the family of PRMTs. The crystal structure of full-length PRMT7 from Mus musculus refined at 1.7 angstrom resolution is described. The PRMT7 structure is composed of two catalytic modules in tandem forming a pseudo-dimer and contains only one AdoHcy molecule bound to the N-terminal module. The high-resolution crystal structure presented here revealed several structural features showing that the second active site is frozen in an inactive state by a conserved zinc finger located at the junction between the two PRMT modules and by the collapse of two degenerated AdoMet-binding loops.
机译：蛋白质精氨酸甲基转移酶7 (PRMT7)类型III的精氨酸甲基转移酶牵涉到一些生物过程如转录调控、DNA损伤修理、RNA拼接、细胞分化和转移。特征PRMTs家族的成员。晶体结构的长篇PRMT7亩进行精制为1.7埃分辨率描述。催化模块串联形成pseudo-dimer和只包含一个AdoHcy分子绑定到n端模块。这里介绍高分辨率的晶体结构揭示了一些结构特点显示第二个活性部位是冻结在一个不活跃的守恒的锌指位于状态两个PRMT模块和之间的连接崩溃的两个退化AdoMet-binding循环。

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