6MM1

Structure of the cysteine-rich region from human EHMT2

6MM1 の概要

• エントリーDOI: 10.2210/pdb6mm1/pdb
• 分子名称: Histone-lysine N-methyltransferase EHMT2, ZINC ION (3 entities in total)
• 機能のキーワード: cysteine-rich region, ring-like, zinc-binding, transferase
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 60979.79

構造登録者

Kerchner, K.M.,Mou, T.C.,Sprang, S.R.,Briknarova, K. (登録日: 2018-09-28, 公開日: 2019-10-02, 最終更新日: 2024-05-22)

主引用文献

Kerchner, K.M.,Mou, T.C.,Sun, Y.,Rusnac, D.V.,Sprang, S.R.,Briknarova, K.
The structure of the cysteine-rich region from human histone-lysine N-methyltransferase EHMT2 (G9a).
J Struct Biol X, 5:100050-100050, 2021

PubMed Abstract: Euchromatic histone-lysine N-methyltransferase 1 (EHMT1; G9a-like protein; GLP) and euchromatic histone-lysine N-methyltransferase 2 (EHMT2; G9a) are protein lysine methyltransferases that regulate gene expression and are essential for development and the ability of organisms to change and adapt. In addition to ankyrin repeats and the catalytic SET domain, the EHMT proteins contain a unique cysteine-rich region (CRR) that mediates protein-protein interactions and recruitment of the methyltransferases to specific sites in chromatin. We have determined the structure of the CRR from human EHMT2 by X-ray crystallography and show that the CRR adopts an unusual compact fold with four bound zinc atoms. The structure consists of a RING domain preceded by a smaller zinc-binding motif and an N-terminal segment. The smaller zinc-binding motif straddles the N-terminal end of the RING domain, and the N-terminal segment runs in an extended conformation along one side of the structure and interacts with both the smaller zinc-binding motif and the RING domain. The interface between the N-terminal segment and the RING domain includes one of the zinc atoms. The RING domain is partially sequestered within the CRR and unlikely to function as a ubiquitin ligase.

PubMed: 34278292
DOI: 10.1016/j.yjsbx.2021.100050

実験手法

X-RAY DIFFRACTION (1.9 Å)