2IGQ

Human euchromatic histone methyltransferase 1

2IGQ の概要

• エントリーDOI: 10.2210/pdb2igq/pdb
• 分子名称: euchromatic histone methyltransferase 1, ZINC ION, S-ADENOSYL-L-HOMOCYSTEINE, ... (4 entities in total)
• 機能のキーワード: euchromatic histone methyltransferase 1, structural genomics, structural genomics consortium, sgc, transferase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus: Q9H9B1
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 66952.53

構造登録者

Min, J.,Wu, H.,Antoshenko, T.,Loppnau, P.,Weigelt, J.,Sundstrom, M.,Arrowsmith, C.H.,Edwards, A.M.,Bochkarev, A.,Plotnikov, A.N.,Structural Genomics Consortium (SGC) (登録日: 2006-09-23, 公開日: 2006-10-24, 最終更新日: 2023-08-30)

主引用文献

Wu, H.,Min, J.,Lunin, V.V.,Antoshenko, T.,Dombrovski, L.,Zeng, H.,Allali-Hassani, A.,Campagna-Slater, V.,Vedadi, M.,Arrowsmith, C.H.,Plotnikov, A.N.,Schapira, M.
Structural biology of human H3K9 methyltransferases
Plos One, 5:e8570-e8570, 2010

PubMed Abstract: SET domain methyltransferases deposit methyl marks on specific histone tail lysine residues and play a major role in epigenetic regulation of gene transcription. We solved the structures of the catalytic domains of GLP, G9a, Suv39H2 and PRDM2, four of the eight known human H3K9 methyltransferases in their apo conformation or in complex with the methyl donating cofactor, and peptide substrates. We analyzed the structural determinants for methylation state specificity, and designed a G9a mutant able to tri-methylate H3K9. We show that the I-SET domain acts as a rigid docking platform, while induced-fit of the Post-SET domain is necessary to achieve a catalytically competent conformation. We also propose a model where long-range electrostatics bring enzyme and histone substrate together, while the presence of an arginine upstream of the target lysine is critical for binding and specificity.

PubMed: 20084102
DOI: 10.1371/journal.pone.0008570

実験手法

X-RAY DIFFRACTION (2 Å)