2AYO

Structure of USP14 bound to ubquitin aldehyde

2AYO の概要

• エントリーDOI: 10.2210/pdb2ayo/pdb
• 関連するPDBエントリー: 2AYN
• 分子名称: Ubiquitin carboxyl-terminal hydrolase 14, Ubiquitin (2 entities in total)
• 機能のキーワード: deubiquitinating enzyme, dub, usp14, proteasome, enzyme mechanism, hydrolase
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cytoplasm: P54578
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 54771.21

構造登録者

Hu, M.,Li, P.,Jeffrey, P.D.,Shi, Y. (登録日: 2005-09-07, 公開日: 2005-10-18, 最終更新日: 2023-11-15)

主引用文献

Hu, M.,Li, P.,Song, L.,Jeffrey, P.D.,Chenova, T.A.,Wilkinson, K.D.,Cohen, R.E.,Shi, Y.
Structure and mechanisms of the proteasome-associated deubiquitinating enzyme USP14.
Embo J., 24:3747-3756, 2005

PubMed Abstract: The ubiquitin-specific processing protease (UBP) family of deubiquitinating enzymes plays an essential role in numerous cellular processes. Mammalian USP14 (Ubp6 in yeast) is unique among known UBP enzymes in that it is activated catalytically upon specific association with the 26S proteasome. Here, we report the crystal structures of the 45-kDa catalytic domain of USP14 in isolation and in a complex with ubiquitin aldehyde, which reveal distinct structural features. In the absence of ubiquitin binding, the catalytic cleft leading to the active site of USP14 is blocked by two surface loops. Binding by ubiquitin induces a significant conformational change that translocates the two surface loops thereby allowing access of the ubiquitin C-terminus to the active site. These structural observations, in conjunction with biochemical characterization, identify important regulatory mechanisms for USP14.

PubMed: 16211010
DOI: 10.1038/sj.emboj.7600832

実験手法

X-RAY DIFFRACTION (3.5 Å)