作者
Xing Zhang, Hisashi Tamaru, Seema I Khan, John R Horton, Lisa J Keefe, Eric U Selker, Xiaodong Cheng
发表日期
2002/10/4
期刊
Cell
卷号
111
期号
1
页码范围
117-127
出版商
Elsevier
简介
AdoMet-dependent methylation of histones is part of the "histone code" that can profoundly influence gene expression. We describe the crystal structure of Neurospora DIM-5, a histone H3 lysine 9 methyltranferase (HKMT), determined at 1.98 Å resolution, as well as results of biochemical characterization and site-directed mutagenesis of key residues. This SET domain protein bears no structural similarity to previously characterized AdoMet-dependent methyltransferases but includes notable features such as a triangular Zn3Cys9 zinc cluster in the pre-SET domain and a AdoMet binding site in the SET domain essential for methyl transfer. The structure suggests a mechanism for the methylation reaction and provides the structural basis for functional characterization of the HKMT family and the SET domain.
引用总数
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