5JTV

USP7CD-UBL45 in complex with Ubiquitin

5JTV の概要

• エントリーDOI: 10.2210/pdb5jtv/pdb
• 関連するPDBエントリー: 5J7T 5JTJ
• 分子名称: Ubiquitin carboxyl-terminal hydrolase 7, Polyubiquitin-B (2 entities in total)
• 機能のキーワード: usp7, hausp, c-terminal activation, hydrolase
• 由来する生物種: Homo sapiens (Human); 詳細
• 細胞内の位置: Nucleus : Q93009; Ubiquitin: Cytoplasm : P0CG47
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 310636.73

構造登録者

Murray, J.M.,Rouge, L. (登録日: 2016-05-09, 公開日: 2016-10-12, 最終更新日: 2023-09-27)

主引用文献

Rouge, L.,Bainbridge, T.W.,Kwok, M.,Tong, R.,Di Lello, P.,Wertz, I.E.,Maurer, T.,Ernst, J.A.,Murray, J.
Molecular Understanding of USP7 Substrate Recognition and C-Terminal Activation.
Structure, 24:1335-1345, 2016

PubMed Abstract: The deubiquitinating enzyme USP7 has a pivotal role in regulating the stability of proteins involved in fundamental cellular processes of normal biology and disease. Despite the importance of USP7, the mechanisms underlying substrate recognition and catalytic activation are poorly understood. Here we present structural, biochemical, and biophysical analyses elucidating the molecular mechanism by which the C-terminal 19 amino acids of USP7 (residues 1084-1102) enhance the ubiquitin cleavage activity of the deubiquitinase (DUB) domain. Our data demonstrate that the C-terminal peptide binds the activation cleft in the catalytic domain and stabilizes the catalytically competent conformation of USP7. Additional structures of longer fragments of USP7, as well as solution studies, provide insight into full-length USP7, the role of the UBL domains, and demonstrate that both substrate recognition and deubiquitinase activity are highly regulated by the catalytic and noncatalytic domains of USP7, a feature that could be essential for the proper function of multi-domain DUBs.

PubMed: 27452404
DOI: 10.1016/j.str.2016.05.020

実験手法

X-RAY DIFFRACTION (3.312 Å)