5TRB

Crystal structure of the RNF20 RING domain

「5DNG」から置き換えられました

5TRB の概要

• エントリーDOI: 10.2210/pdb5trb/pdb
• 分子名称: E3 ubiquitin-protein ligase BRE1A, ZINC ION (3 entities in total)
• 機能のキーワード: ligase
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Nucleus : Q5VTR2
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8846.07

構造登録者

Foglizzo, M.,Middleton, A.J.,Day, C.L. (登録日: 2016-10-25, 公開日: 2016-11-02, 最終更新日: 2024-03-06)

主引用文献

Foglizzo, M.,Middleton, A.J.,Day, C.L.
Structure and Function of the RING Domains of RNF20 and RNF40, Dimeric E3 Ligases that Monoubiquitylate Histone H2B.
J.Mol.Biol., 428:4073-4086, 2016

PubMed Abstract: Monoubiquitylation of histone H2B is a post-translational mark that plays key roles in regulation of transcription and genome stability. In humans, attachment of ubiquitin to lysine 120 of histone H2B depends on the activity of the E2 ubiquitin-conjugating enzyme, Ube2B, and the really interesting new gene (RING) E3 ligases, RING finger protein (RNF) 20 and RNF40. To better understand the molecular basis of this modification, we have solved the crystal structure of the RNF20 RING domain and show that it is a homodimer that specifically interacts with the Ube2B~Ub conjugate. By mutating residues at the E3-E2 and E3-ubiquitin interfaces, we identify key contacts required for interaction of the RNF20 RING domain with the Ube2B~Ub conjugate. These mutants were used to generate a structure-based model of the RNF20-Ube2B~Ub complex that reveals differences from other RING-E2~Ub complexes, and suggests how the RNF20-Ube2B~Ub complex might interact with its nucleosomal substrate. Additionally, we show that the RING domains of RNF20 and RNF40 can form a stable heterodimer that is active. Together, our studies provide new insights into the mechanisms that regulate RNF20-mediated ubiquitin transfer from Ube2B.

PubMed: 27569044
DOI: 10.1016/j.jmb.2016.07.025

実験手法

X-RAY DIFFRACTION (1.8 Å)