Crystal Structure of the 2-Oxoglutarate- and Fe(II)-Dependent Lysyl Hydroxylase JMJD6
Crystal Structure of the 2-Oxoglutarate- and Fe(II)-Dependent Lysyl Hydroxylase JMJD6
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DOI：
10.1016/j.jmb.2010.05.054
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发表时间：
2010-08-13
影响因子：
5.6
通讯作者：
Schofield, Christopher J.
中科院分区：
文献类型：
--
作者：
Mantri, Monica;Krojer, Tobias;Schofield, Christopher J.
赖氨酰和脯氨酰羟基化是对具有细胞外作用的动物和植物蛋白的众所周知的翻译后修饰。最近的研究表明，细胞内动物蛋白的羟基化可能是常见的。JMJD 6催化RNA剪接相关蛋白的富含精氨酸丝氨酸结构域中赖氨酰残基的铁和2-酮戊二酸依赖性羟基化。我们报告晶体学研究的催化域的JMJD 6在复杂的Ni（II）取代Fe（II）。与突变研究一起，结构数据表明JMJD 6如何结合其赖氨酰残基，使得它可以催化C-5羟基化，而不是类似酶的N-脱甲基化。(C)2010爱思唯尔有限公司版权所有。
Lysyl and prolyl hydroxylations are well-known post-translational modifications to animal and plant proteins with extracellular roles. More recent work has indicated that the hydroxylation of intracellular animal proteins may be common. JMJD6 catalyses the iron- and 2-oxoglutarate-dependent hydroxylation of lysyl residues in arginine serine-rich domains of RNA-splicing-related proteins. We report crystallographic studies on the catalytic domain of JMJD6 in complex with Ni(II) substituting for Fe(II). Together with mutational studies, the structural data suggest how JMJD6 binds its lysyl residues such that it can catalyse C-5 hydroxylation rather than N-epsilon-demethylation, as for analogous enzymes. (C) 2010 Elsevier Ltd. All rights reserved.