1H3I

Crystal structure of the Histone Methyltransferase SET7/9

1H3I の概要

• エントリーDOI: 10.2210/pdb1h3i/pdb
• 分子名称: HISTONE H3 LYSINE 4 SPECIFIC METHYLTRANSFERASE, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: transferase, methyltransferase
• 由来する生物種: HOMO SAPIENS (HUMAN)
• 細胞内の位置: Nucleus: Q8WTS6
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 65216.74

構造登録者

Wilson, J.R.,Jing, C.,Walker, P.A.,Martin, S.R.,Howell, S.A.,Blackburn, G.M.,Gamblin, S.J.,Xiao, B. (登録日: 2002-09-04, 公開日: 2002-11-11, 最終更新日: 2024-05-08)

主引用文献

Wilson, J.R.,Jing, C.,Walker, P.A.,Martin, S.R.,Howell, S.A.,Blackburn, G.M.,Gamblin, S.J.,Xiao, B.
Crystal Structure and Functional Analysis of the Histone Methyltransferase Set7/9
Cell(Cambridge,Mass.), 111:105-, 2002

PubMed Abstract: 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.

PubMed: 12372304
DOI: 10.1016/S0092-8674(02)00964-9

実験手法

X-RAY DIFFRACTION (2.1 Å)