2DOS

Structural basis for the recognition of Lys48-linked polyubiquitin chain by the Josephin domain of ataxin-3, a putative deubiquitinating enzyme

2DOS の概要

• エントリーDOI: 10.2210/pdb2dos/pdb
• 分子名称: Ataxin-3 (1 entity in total)
• 機能のキーワード: deubiquitinating enzyme, hydrolase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus matrix : P54252
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20162.67

構造登録者

Sumiyoshi, A. (登録日: 2006-05-03, 公開日: 2007-05-22, 最終更新日: 2024-05-01)

主引用文献

Satoh, T.,Sumiyoshi, A.,Yagi-Utsumi, M.,Sakata, E.,Sasakawa, H.,Kurimoto, E.,Yamaguchi, Y.,Li, W.,Joazeiro, C.A.,Hirokawa, T.,Kato, K.
Mode of substrate recognition by the Josephin domain of ataxin-3, which has an endo-type deubiquitinase activity.
Febs Lett., 588:4422-4430, 2014

PubMed Abstract: Ataxin-3, which is encoded by a gene that has been associated with Machado-Joseph disease, contains a catalytic N-terminal Josephin domain with deubiquitinase activity. Here, we show that the Josephin domain of ataxin 3 catalyzes endo-type cleavage of Lys48-linked polyubiquitin. Furthermore, NMR data obtained following site-specific paramagnetic spin labeling of Lys48-linked di-ubiquitin revealed that both ubiquitin units interact with the Josephin domain, with the C-terminal Gly76 of the proximal unit being situated in the vicinity of the catalytic triad of Josephin domain. Our results help to elucidate how the substrate is recognized by the Josephin domain and properly positioned for an endo-type deubiquitination reaction.

PubMed: 25448680
DOI: 10.1016/j.febslet.2014.10.013

実験手法

SOLUTION NMR