6WW3

Crystal structure of HERC2 ZZ domain in complex with SUMO1 tail

6WW3 の概要

• エントリーDOI: 10.2210/pdb6ww3/pdb
• 分子名称: SUMO1 linked HERC2 ZZ domain (Small ubiquitin-related modifier 1,E3 ubiquitin-protein ligase HERC2), ZINC ION, DI(HYDROXYETHYL)ETHER, ... (5 entities in total)
• 機能のキーワード: zn finger protein, zz domain, herc2, gene regulation
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 14279.38

構造登録者

Liu, J.,Vann, K.R.,Kutateladze, T.G. (登録日: 2020-05-07, 公開日: 2020-08-05, 最終更新日: 2023-10-18)

主引用文献

Liu, J.,Xue, Z.,Zhang, Y.,Vann, K.R.,Shi, X.,Kutateladze, T.G.
Structural Insight into Binding of the ZZ Domain of HERC2 to Histone H3 and SUMO1.
Structure, 28:1225-1230.e3, 2020

PubMed Abstract: Human ubiquitin ligase HERC2, a component of the DNA repair machinery, has been linked to neurological diseases and cancer. Here, we show that the ZZ domain of HERC2 (HERC2) binds to histone H3 tail and tolerates posttranslational modifications commonly present in H3. The crystal structure of the HERC2:H3 complex provides the molecular basis for this interaction and highlights a critical role of the negatively charged site of HERC2 in capturing of A1 of H3. NMR, mutagenesis, and fluorescence data reveal that HERC2 binds to H3 and the N-terminal tail of SUMO1, a previously reported ligand of HERC2, with comparable affinities. Like H3, the N-terminal tail of SUMO1 occupies the same negatively charged site of HERC2 in the crystal structure of the complex, although in contrast to H3 it adopts an α-helical conformation. Our data suggest that HERC2 may play a role in mediating the association of HERC2 with chromatin.

PubMed: 32726574
DOI: 10.1016/j.str.2020.07.003

実験手法

X-RAY DIFFRACTION (2.096 Å)