2XEU

Ring domain

2XEU の概要

• エントリーDOI: 10.2210/pdb2xeu/pdb
• 関連するBIRD辞書のPRD_ID: PRD_900003
• 分子名称: RING FINGER PROTEIN 4, beta-D-fructofuranose-(2-1)-alpha-D-glucopyranose, ZINC ION, ... (5 entities in total)
• 機能のキーワード: transcription, zinc-finger, metal-binding
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 7880.70

構造登録者

Plechanovova, A.,McMahon, S.A.,Johnson, K.A.,Navratilova, I.,Naismith, J.H.,Hay, R.T. (登録日: 2010-05-18, 公開日: 2010-07-28, 最終更新日: 2024-05-08)

主引用文献

Plechanovova, A.,Jaffray, E.G.,Mcmahon, S.A.,Johnson, K.A.,Navratilova, I.,Naismith, J.H.,Hay, R.T.
Mechanism of Ubiquitylation by Dimeric Ring Ligase Rnf4
Nat.Struct.Mol.Biol., 18:1052-, 2011

PubMed Abstract: Mammalian RNF4 is a dimeric RING ubiquitin E3 ligase that ubiquitylates poly-SUMOylated proteins. We found that RNF4 bound ubiquitin-charged UbcH5a tightly but free UbcH5a weakly. To provide insight into the mechanism of RING-mediated ubiquitylation, we docked the UbcH5~ubiquitin thioester onto the RNF4 RING structure. This revealed that with E2 bound to one monomer of RNF4, the thioester-linked ubiquitin could reach across the dimer to engage the other monomer. In this model, the 'Ile44 hydrophobic patch' of ubiquitin is predicted to engage a conserved tyrosine located at the dimer interface of the RING, and mutation of these residues blocked ubiquitylation activity. Thus, dimeric RING ligases are not simply inert scaffolds that bring substrate and E2-loaded ubiquitin into close proximity. Instead, they facilitate ubiquitin transfer by preferentially binding the E2~ubiquitin thioester across the dimer and activating the thioester bond for catalysis.

PubMed: 21857666
DOI: 10.1038/NSMB.2108

実験手法

X-RAY DIFFRACTION (1.5 Å)