1h3i

From Proteopedia

Revision as of 14:22, 5 November 2007

CRYSTAL STRUCTURE OF THE HISTONE METHYLTRANSFERASE SET7/9

Overview

Methylation of lysine residues in the N-terminal tails of histones is, thought to represent an important component of the mechanism that, regulates chromatin structure. The evolutionarily conserved SET domain, occurs in most proteins known to possess histone lysine methyltransferase, activity. We present here the crystal structure of a large fragment of, human SET7/9 that contains a N-terminal beta-sheet domain as well as the, conserved SET domain. Mutagenesis identifies two residues in the C, terminus of the protein that appear essential for catalytic activity, toward lysine-4 of histone H3. Furthermore, we show how the cofactor, AdoMet binds to this domain and present biochemical data supporting the, role of invariant residues in catalysis, binding of AdoMet, and, interactions with the peptide substrate.

About this Structure

1H3I is a Single protein structure of sequence from Homo sapiens with MG as ligand. Active as Histone-lysine N-methyltransferase, with EC number 2.1.1.43 Structure known Active Site: AC1. Full crystallographic information is available from OCA.

Reference

Crystal structure and functional analysis of the histone methyltransferase SET7/9., Wilson JR, Jing C, Walker PA, Martin SR, Howell SA, Blackburn GM, Gamblin SJ, Xiao B, Cell. 2002 Oct 4;111(1):105-15. PMID:12372304

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