2YBF

Complex of Rad18 (Rad6 binding domain) with Rad6b

2YBF の概要

• エントリーDOI: 10.2210/pdb2ybf/pdb
• 関連するPDBエントリー: 1JAS 1NXA 2Y43 2Y4W 2YB6
• 分子名称: UBIQUITIN-CONJUGATING ENZYME E2 B, E3 UBIQUITIN-PROTEIN LIGASE RAD18, BETA-MERCAPTOETHANOL, ... (6 entities in total)
• 機能のキーワード: ligase, e2 ubiquitin conjugating enzyme, e3 ubiquitin ligase, translesion synthesis, pcna ubiquitination
• 由来する生物種: HOMO SAPIENS (HUMAN); 詳細
• 細胞内の位置: Cell membrane (By similarity): P63146; Nucleus (By similarity): Q9NS91
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 20839.34

構造登録者

Hibbert, R.G.,Sixma, T.K. (登録日: 2011-03-08, 公開日: 2011-04-20, 最終更新日: 2023-12-20)

主引用文献

Hibbert, R.G.,Huang, A.,Boelens, R.,Sixma, T.K.
E3 Ligase Rad18 Promotes Monoubiquitination Rather Than Ubiquitin Chain Formation by E2 Enzyme Rad6.
Proc.Natl.Acad.Sci.USA, 108:5590-, 2011

PubMed Abstract: In ubiquitin conjugation, different combinations of E2 and E3 enzymes catalyse either monoubiquitination or ubiquitin chain formation. The E2/E3 complex Rad6/Rad18 exclusively monoubiquitinates the proliferating cell nuclear antigen (PCNA) to signal for "error prone" DNA damage tolerance, whereas a different set of conjugation enzymes is required for ubiquitin chain formation on PCNA. Here we show that human E2 enzyme Rad6b is intrinsically capable of catalyzing ubiquitin chain formation. This activity is prevented during PCNA ubiquitination by the interaction of Rad6 with E3 enzyme Rad18. Using NMR and X-ray crystallography we show that the R6BD of Rad18 inhibits this activity by competing with ubiquitin for a noncovalent "backside" binding site on Rad6. Our findings provide mechanistic insights into how E3 enzymes can regulate the ubiquitin conjugation process.

PubMed: 21422291
DOI: 10.1073/PNAS.1017516108

実験手法

X-RAY DIFFRACTION (2 Å)