7R71

Crystal Structure of the UbArk2C-UbcH5b~Ub complex

7R71 の概要

• エントリーDOI: 10.2210/pdb7r71/pdb
• 分子名称: Ubiquitin,E3 ubiquitin-protein ligase RNF165, Ubiquitin, Ubiquitin-conjugating enzyme E2 D2, ... (4 entities in total)
• 機能のキーワード: ring e3 ligase ubiquitin ptm, ligase, e2~ub conjugate, transferase
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 46259.40

構造登録者

Paluda, A.,Middleton, A.J.,Mace, P.D.,Day, C.L. (登録日: 2021-06-24, 公開日: 2022-03-09, 最終更新日: 2024-11-20)

主引用文献

Paluda, A.,Middleton, A.J.,Rossig, C.,Mace, P.D.,Day, C.L.
Ubiquitin and a charged loop regulate the ubiquitin E3 ligase activity of Ark2C.
Nat Commun, 13:1181-1181, 2022

PubMed Abstract: A large family of E3 ligases that contain both substrate recruitment and RING domains confer specificity within the ubiquitylation cascade. Regulation of RING E3s depends on modulating their ability to stabilise the RING bound E2~ubiquitin conjugate in the activated (or closed) conformation. Here we report the structure of the Ark2C RING bound to both a regulatory ubiquitin molecule and an activated E2~ubiquitin conjugate. The structure shows that the RING domain and non-covalently bound ubiquitin molecule together make contacts that stabilise the activated conformation of the conjugate, revealing why ubiquitin is a key regulator of Ark2C activity. We also identify a charged loop N-terminal to the RING domain that enhances activity by interacting with both the regulatory ubiquitin and ubiquitin conjugated to the E2. In addition, the structure suggests how Lys48-linked ubiquitin chains might be assembled by Ark2C and UbcH5b. Together this study identifies features common to RING E3s, as well elements that are unique to Ark2C and related E3s, which enhance assembly of ubiquitin chains.

PubMed: 35246518
DOI: 10.1038/s41467-022-28782-y

実験手法

X-RAY DIFFRACTION (2.8 Å)