8GCB

Structure of RNF125 in complex with a UbcH5b~Ub conjugate

8GCB の概要

• エントリーDOI: 10.2210/pdb8gcb/pdb
• 分子名称: Ubiquitin-conjugating enzyme E2 D2, E3 ubiquitin-protein ligase RNF125, ZINC ION (3 entities in total)
• 機能のキーワード: ubiquitin ring e3 ligase ubiquitin conjugating enzyme complex, ligase
• 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: 28756.09

構造登録者

Middleton, A.J.,Day, C.L.,Fokkens, T.J. (登録日: 2023-03-01, 公開日: 2023-07-19, 最終更新日: 2023-10-18)

主引用文献

Middleton, A.J.,Barzak, F.M.,Fokkens, T.J.,Nguyen, K.,Day, C.L.
Zinc finger 1 of the RING E3 ligase, RNF125, interacts with the E2 to enhance ubiquitylation.
Structure, 31:1208-1219.e5, 2023

PubMed Abstract: Inflammation is essential for healthy immune function, wound healing, and resolution of infection. RIG-I is a key RNA sensor that initiates an immune response, with activation and termination of RIG-I signaling reliant on its modification with ubiquitin. The RING E3 ubiquitin ligase, RNF125, has a critical role in the attenuation of RIG-I signaling, yet it is not known how RNF125 promotes ubiquitin transfer or how its activity is regulated. Here we show that the E3 ligase activity of RNF125 relies on the first zinc finger (ZF1) as well as the RING domain. Surprisingly, ZF1 helps recruit the E2, while residues N-terminal to the RING domain appear to activate the E2∼Ub conjugate. These discoveries help explain how RNF125 brings about the termination of RIG-I dependent inflammatory responses, and help account for the contribution of RNF125 to disease. This study also reveals a new role for ZF domains in E3 ligases.

PubMed: 37541247
DOI: 10.1016/j.str.2023.07.007

実験手法

X-RAY DIFFRACTION (2.39 Å)