Structure of the Neurospora SET domain protein DIM-5, a histone H3 lysine methyltransferase.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 12372305.
- Also identified by PMC identifier 2713760.
- No licence information is recorded for this record.
- Because redistribution is not established, this page shows the abstract only. Follow the links below for the full text.
Abstract
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.
Medical subject headings
- DNA-Binding Proteins
- Drosophila Proteins
- Histone-Lysine N-Methyltransferase
- Histones
- Methyltransferases
- Neurospora
- Nuclear Proteins
- Repressor Proteins
- Transcription Factors