1NBF

Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde

1NBF の概要

• エントリーDOI: 10.2210/pdb1nbf/pdb
• 関連するPDBエントリー: 1NB8
• 分子名称: Ubiquitin carboxyl-terminal hydrolase 7, Ubiquitin aldehyde (3 entities in total)
• 機能のキーワード: deubiquitinating enzyme, hausp, ubiquitin binding, catalytic mechanisms of upbs, hydrolase
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 140134.68

構造登録者

Hu, M.,Li, P.,Li, M.,Li, W.,Yao, T.,Wu, J.-W.,Gu, W.,Cohen, R.E.,Shi, Y. (登録日: 2002-12-02, 公開日: 2003-01-07, 最終更新日: 2025-03-26)

主引用文献

Hu, M.,Li, P.,Li, M.,Li, W.,Yao, T.,Wu, J.-W.,Gu, W.,Cohen, R.E.,Shi, Y.
Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde
Cell(Cambridge,Mass.), 111:1041-1054, 2002

PubMed Abstract: The ubiquitin-specific processing protease (UBP) family of deubiquitinating enzymes plays an essential role in numerous cellular processes. HAUSP, a representative UBP, specifically deubiquitinates and hence stabilizes the tumor suppressor protein p53. Here, we report the crystal structures of the 40 kDa catalytic core domain of HAUSP in isolation and in complex with ubiquitin aldehyde. These studies reveal that the UBP deubiquitinating enzymes exhibit a conserved three-domain architecture, comprising Fingers, Palm, and Thumb. The leaving ubiquitin moiety is specifically coordinated by the Fingers, with its C terminus placed in the active site between the Palm and the Thumb. Binding by ubiquitin aldehyde induces a drastic conformational change in the active site that realigns the catalytic triad residues for catalysis.

PubMed: 12507430
DOI: 10.1016/S0092-8674(02)01199-6

実験手法

X-RAY DIFFRACTION (2.3 Å)