3B95

EuHMT1 (Glp) Ankyrin Repeat Domain (Structure 2)

3B95 の概要

• エントリーDOI: 10.2210/pdb3b95/pdb
• 関連するPDBエントリー: 3B7B
• 分子名称: Euchromatic histone-lysine N-methyltransferase 1, Histone H3 N-terminal Peptide, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: ankyrin repeat, ank repeat, methyltransferase, transferase, transferase-structural protein complex, transferase/structural protein
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 54904.77

構造登録者

Collins, R.E.,Horton, J.R.,Cheng, X. (登録日: 2007-11-02, 公開日: 2008-02-12, 最終更新日: 2023-08-30)

主引用文献

Collins, R.E.,Northrop, J.P.,Horton, J.R.,Lee, D.Y.,Zhang, X.,Stallcup, M.R.,Cheng, X.
The ankyrin repeats of G9a and GLP histone methyltransferases are mono- and dimethyllysine binding modules.
Nat.Struct.Mol.Biol., 15:245-250, 2008

PubMed Abstract: Histone modifications have important roles in transcriptional control, mitosis and heterochromatin formation. G9a and G9a-like protein (GLP) are euchromatin-associated methyltransferases that repress transcription by mono- and dimethylating histone H3 at Lys9 (H3K9). Here we demonstrate that the ankyrin repeat domains of G9a and GLP bind with strong preference to N-terminal H3 peptides containing mono- or dimethyl K9. X-ray crystallography revealed the basis for recognition of the methylated lysine by a partial hydrophobic cage with three tryptophans and one acidic residue. Substitution of key residues in the cage eliminated the H3 tail interaction. Hence, G9a and GLP contain a new type of methyllysine binding module (the ankyrin repeat domains) and are the first examples of protein (histone) methyltransferases harboring in a single polypeptide the activities that generate and read the same epigenetic mark.

PubMed: 18264113
DOI: 10.1038/nsmb.1384

実験手法

X-RAY DIFFRACTION (2.99 Å)