4FK5

Structure of the SAGA Ubp8(S144N)/Sgf11/Sus1/Sgf73 DUB module

4FK5 の概要

• エントリーDOI: 10.2210/pdb4fk5/pdb
• 関連するPDBエントリー: 4FIP 4FJC
• 分子名称: Ubiquitin carboxyl-terminal hydrolase 8, Protein SUS1, SAGA-associated factor 11, ... (8 entities in total)
• 機能のキーワード: multi-protein complex, deubiquitination, transcription, nucleosome, hydrolase
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast); 詳細
• 細胞内の位置: Nucleus (Probable): P50102 Q03067 P53165; Nucleus, nucleoplasm: Q6WNK7
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 88046.58

構造登録者

Samara, N.L.,Ringel, A.E.,Wolberger, C. (登録日: 2012-06-12, 公開日: 2012-07-25, 最終更新日: 2024-02-28)

主引用文献

Samara, N.L.,Ringel, A.E.,Wolberger, C.
A Role for Intersubunit Interactions in Maintaining SAGA Deubiquitinating Module Structure and Activity.
Structure, 20:1414-1424, 2012

PubMed Abstract: The deubiquitinating module (DUBm) of the SAGA coactivator contains the Ubp8 isopeptidase, Sgf11, Sus1, and Sgf73, which form a highly interconnected complex. Although Ubp8 contains a canonical USP catalytic domain, it is only active when in complex with the other DUBm subunits. The Sgf11 zinc finger (Sgf11-ZnF) binds near the Ubp8 active site and is essential for full activity, suggesting that the Sgf11-ZnF helps maintain the active conformation of Ubp8. We report structural and solution studies showing that deletion of the Sgf11-ZnF destabilizes incorporation of Ubp8 within the DUBm, giving rise to domain swapping with a second complex and misaligning active site residues. Activating mutations in Ubp8 that partially restore activity in the absence of the Sgf11-ZnF promote the monomeric form of the DUBm. Our data suggest an unexpected role for Sgf11 in compensating for the absence of structural features that maintain the active conformation of Ubp8.

PubMed: 22771212
DOI: 10.1016/j.str.2012.05.015

実験手法

X-RAY DIFFRACTION (2.032 Å)