5FER

Complex of TRIM25 RING with UbcH5-Ub

5FER の概要

• エントリーDOI: 10.2210/pdb5fer/pdb
• 分子名称: E3 ubiquitin/ISG15 ligase TRIM25, Ubiquitin-conjugating enzyme E2 D1, Ubiquitin-40S ribosomal protein S27a, ... (5 entities in total)
• 機能のキーワード: e3 ligase, ubiquitin, ligase
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 69827.36

構造登録者

Rittinger, K.,Koliopoulos, M.G.,Esposito, D. (登録日: 2015-12-17, 公開日: 2016-05-18, 最終更新日: 2024-05-08)

主引用文献

Koliopoulos, M.G.,Esposito, D.,Christodoulou, E.,Taylor, I.A.,Rittinger, K.
Functional role of TRIM E3 ligase oligomerization and regulation of catalytic activity.
Embo J., 35:1204-1218, 2016

PubMed Abstract: TRIM E3 ubiquitin ligases regulate a wide variety of cellular processes and are particularly important during innate immune signalling events. They are characterized by a conserved tripartite motif in their N-terminal portion which comprises a canonical RING domain, one or two B-box domains and a coiled-coil region that mediates ligase dimerization. Self-association via the coiled-coil has been suggested to be crucial for catalytic activity of TRIMs; however, the precise molecular mechanism underlying this observation remains elusive. Here, we provide a detailed characterization of the TRIM ligases TRIM25 and TRIM32 and show how their oligomeric state is linked to catalytic activity. The crystal structure of a complex between the TRIM25 RING domain and an ubiquitin-loaded E2 identifies the structural and mechanistic features that promote a closed E2~Ub conformation to activate the thioester for ubiquitin transfer allowing us to propose a model for the regulation of activity in the full-length protein. Our data reveal an unexpected diversity in the self-association mechanism of TRIMs that might be crucial for their biological function.

PubMed: 27154206
DOI: 10.15252/embj.201593741

実験手法

X-RAY DIFFRACTION (2.34 Å)