Ontology highlight
ABSTRACT:
SUBMITTER: Zhang X
PROVIDER: S-EPMC2713760 | biostudies-literature | 2002 Oct
REPOSITORIES: biostudies-literature
Zhang Xing X Tamaru Hisashi H Khan Seema I SI Horton John R JR Keefe Lisa J LJ Selker Eric U EU Cheng Xiaodong X
Cell 20021001 1
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 A 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 ...[more]