5D0M

Structure of UbE2D2:RNF165:Ub complex

5D0M の概要

• エントリーDOI: 10.2210/pdb5d0m/pdb
• 関連するPDBエントリー: 5D0I 5D0K
• 分子名称: Ubiquitin-conjugating enzyme E2 D2, RING finger protein 165, Polyubiquitin-B, ... (6 entities in total)
• 機能のキーワード: complex, ubiquitin, ligase
• 由来する生物種: Homo sapiens (Human); 詳細
• 細胞内の位置: Ubiquitin: Cytoplasm : P0CG47
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 35816.36

構造登録者

Wright, J.D.,Day, C.L.,Mace, P.D. (登録日: 2015-08-03, 公開日: 2015-12-09, 最終更新日: 2024-11-13)

主引用文献

Wright, J.D.,Mace, P.D.,Day, C.L.
Secondary ubiquitin-RING docking enhances Arkadia and Ark2C E3 ligase activity.
Nat.Struct.Mol.Biol., 23:45-52, 2016

PubMed Abstract: RING-domain E3 ligases enhance transfer of ubiquitin to substrate proteins by stabilizing the RING-bound thioester-linked E2∼ubiquitin conjugate in a defined conformation that primes the active site for nucleophilic attack. Here we report that the monomeric RING domains from the human E3 ligases Arkadia and Ark2C bind directly to free ubiquitin with an affinity comparable to that of other dedicated ubiquitin-binding domains. Further work showed that the Ark-like RING domain and the noncovalently bound ubiquitin molecule coordinately stabilize the E2-conjugated ubiquitin (donor ubiquitin) in the 'closed' conformation. Our studies identify the RING domain of Arkadia as a ubiquitin-binding domain and provide insight into a new ubiquitin-dependent mechanism used by monomeric RING domains to activate ubiquitin transfer. This study also suggests how substrates that have been monoubiquitinated could be favored for further ubiquitination.

PubMed: 26656854
DOI: 10.1038/nsmb.3142

実験手法

X-RAY DIFFRACTION (1.913 Å)