2G45

Co-crystal structure of znf ubp domain from the deubiquitinating enzyme isopeptidase T (isot) in complex with ubiquitin

2G45 の概要

• エントリーDOI: 10.2210/pdb2g45/pdb
• 関連するPDBエントリー: 2G43
• 分子名称: Ubiquitin carboxyl-terminal hydrolase 5, Ubiquitin, ZINC ION, ... (5 entities in total)
• 機能のキーワード: ubiquitin, zinc finger, deubiquitinating enzyme, hydrolase
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 46506.71

構造登録者

Reyes-Turcu, F.E.,Horton, J.R.,Mullally, J.E.,Heroux, A.,Cheng, X.,Wilkinson, K.D. (登録日: 2006-02-21, 公開日: 2006-04-04, 最終更新日: 2024-11-13)

主引用文献

Reyes-Turcu, F.E.,Horton, J.R.,Mullally, J.E.,Heroux, A.,Cheng, X.,Wilkinson, K.D.
The Ubiquitin Binding Domain ZnF UBP Recognizes the C-Terminal Diglycine Motif of Unanchored Ubiquitin.
Cell(Cambridge,Mass.), 124:1197-1208, 2006

PubMed Abstract: Ubiquitin binding proteins regulate the stability, function, and/or localization of ubiquitinated proteins. Here we report the crystal structures of the zinc-finger ubiquitin binding domain (ZnF UBP) from the deubiquitinating enzyme isopeptidase T (IsoT, or USP5) alone and in complex with ubiquitin. Unlike other ubiquitin binding domains, this domain contains a deep binding pocket where the C-terminal diglycine motif of ubiquitin is inserted, thus explaining the specificity of IsoT for an unmodified C terminus on the proximal subunit of polyubiquitin. Mutations in the domain demonstrate that it is required for optimal catalytic activation of IsoT. This domain is present in several other protein families, and the ZnF UBP domain from an E3 ligase also requires the C terminus of ubiquitin for binding. These data suggest that binding the ubiquitin C terminus may be necessary for the function of other proteins.

PubMed: 16564012
DOI: 10.1016/j.cell.2006.02.038

実験手法

X-RAY DIFFRACTION (1.99 Å)