5AIT

A complex of of RNF4-RING domain, UbeV2, Ubc13-Ub (isopeptide crosslink)

5AIT の概要

• エントリーDOI: 10.2210/pdb5ait/pdb
• 分子名称: E3 UBIQUITIN-PROTEIN LIGASE RNF4, UBIQUITIN-CONJUGATING ENZYME E2 N, POLYUBIQUITIN-C, ... (5 entities in total)
• 機能のキーワード: ligase-signaling protein complex, complex, ligase/signaling protein
• 由来する生物種: RATTUS NORVEGICUS (NORWAY RAT); 詳細
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 99698.84

構造登録者

Branigan, E.,Naismith, J.H. (登録日: 2015-02-17, 公開日: 2015-07-08, 最終更新日: 2024-05-08)

主引用文献

Branigan, E.,Plechanovova, A.,Jaffray, E.,Naismith, J.H.,Hay, R.T.
Structural Basis for the Ring Catalyzed Synthesis of K63 Linked Ubiquitin Chains
Nat.Struct.Mol.Biol., 22:597-, 2015

PubMed Abstract: RING E3 ligase-catalyzed formation of K63-linked ubiquitin chains by the Ube2V2-Ubc13 E2 complex is required in many important biological processes. Here we report the structure of the RING-domain dimer of rat RNF4 in complex with a human Ubc13∼Ub conjugate and Ube2V2. The structure has captured Ube2V2 bound to the acceptor (priming) ubiquitin with K63 in a position favorable for attack on the linkage between Ubc13 and the donor (second) ubiquitin held in the active 'folded back' conformation by the RING domain of RNF4. We verified the interfaces identified in the structure by in vitro ubiquitination assays of site-directed mutants. To our knowledge, this represents the first view of synthesis of K63-linked ubiquitin chains in which both substrate ubiquitin and ubiquitin-loaded E2 are juxtaposed to allow E3 ligase-mediated catalysis.

PubMed: 26148049
DOI: 10.1038/NSMB.3052

実験手法

X-RAY DIFFRACTION (3.4 Å)