7W3R

USP34 catalytic domain

7W3R の概要

• エントリーDOI: 10.2210/pdb7w3r/pdb
• 分子名称: Ubiquitin carboxyl-terminal hydrolase 34, ZINC ION (3 entities in total)
• 機能のキーワード: usp34 in isolation, hydrolase
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 89861.02

構造登録者

Xu, G.L.,Ming, Z.H. (登録日: 2021-11-26, 公開日: 2022-06-01, 最終更新日: 2023-11-29)

主引用文献

Xu, G.,Su, H.,Lu, L.,Liu, X.,Zhao, L.,Tang, B.,Ming, Z.
Structural Insights into the Catalytic Mechanism and Ubiquitin Recognition of USP34.
J.Mol.Biol., 434:167634-167634, 2022

PubMed Abstract: Ubiquitination, an important posttranslational modification, participates in virtually all aspects of cellular functions and is reversed by deubiquitinating enzymes (DUBs). Ubiquitin-specific protease 34 (USP34) plays an essential role in cancer, neurodegenerative diseases, and osteogenesis. Despite its functional importance, how USP34 recognizes ubiquitin and catalyzes deubiquitination remains structurally uncharacterized. Here, we report the crystal structures of the USP34 catalytic domain in free state and after binding with ubiquitin. In the free state, USP34 adopts an inactive conformation, which contains a misaligned catalytic histidine in the triad. Comparison of USP34 structures before and after ubiquitin binding reveals a structural basis for ubiquitin recognition and elucidates a mechanism by which the catalytic triad is realigned. Transition from an open inactive state to a relatively closed active state is coupled to a process by which the "fingertips" of USP34 intimately grip ubiquitin, and this has not been reported before. Our structural and biochemical analyses provide important insights into the catalytic mechanism and ubiquitin recognition of USP34.

PubMed: 35588869
DOI: 10.1016/j.jmb.2022.167634

実験手法

X-RAY DIFFRACTION (1.92 Å)