1ml9 | pdb_00001ml9
Structure of the Neurospora SET domain protein DIM-5, a histone lysine methyltransferase
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Overview
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 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.
About this Structure
1ML9 is a Single protein structure of sequence from Neurospora crassa with ZN and UNK as ligands. Active as Histone-lysine N-methyltransferase, with EC number 2.1.1.43 Full crystallographic information is available from OCA.
Reference
Structure of the Neurospora SET domain protein DIM-5, a histone H3 lysine methyltransferase., Zhang X, Tamaru H, Khan SI, Horton JR, Keefe LJ, Selker EU, Cheng X, Cell. 2002 Oct 4;111(1):117-27. PMID:12372305
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