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2LBC

solution structure of tandem UBA of USP13

2LBC の概要
エントリーDOI10.2210/pdb2lbc/pdb
NMR情報BMRB: 17554
分子名称Ubiquitin carboxyl-terminal hydrolase 13 (1 entity in total)
機能のキーワードtandem uba of usp13, hydrolase
由来する生物種Homo sapiens (human)
タンパク質・核酸の鎖数1
化学式量合計13769.25
構造登録者
Zhang, Y.,Zhou, C.,Zhou, Z.,Song, A.,Hu, H. (登録日: 2011-03-29, 公開日: 2012-03-07, 最終更新日: 2024-05-15)
主引用文献Zhang, Y.,Zhou, C.,Zhou, Z.,Song, A.,Hu, H.
Domain Analysis Reveals That a Deubiquitinating Enzyme USP13 Performs Non-Activating Catalysis for Lys63-Linked Polyubiquitin.
Plos One, 6:e29362-e29362, 2011
Cited by
PubMed Abstract: Deubiquitination is a reverse process of cellular ubiquitination important for many biological events. Ubiquitin (Ub)-specific protease 13 (USP13) is an ortholog of USP5 implicated in catalyzing hydrolysis of various Ub chains, but its enzymatic properties and catalytic regulation remain to be explored. Here we report studies of the roles of the Ub-binding domains of USP13 in regulatory catalysis by biochemical and NMR structural approaches. Our data demonstrate that USP13, distinct from USP5, exhibits a weak deubiquitinating activity preferring to Lys63-linked polyubiquitin (K63-polyUb) in a non-activation manner. The zinc finger (ZnF) domain of USP13 shares a similar fold with that of USP5, but it cannot bind with Ub, so that USP13 has lost its ability to be activated by free Ub. Substitution of the ZnF domain with that of USP5 confers USP13 the property of catalytic activation. The tandem Ub-associated (UBA) domains of USP13 can bind with different types of diUb but preferentially with K63-linked, providing a possible explanation for the weak activity preferring to K63-polyUb. USP13 can also regulate the protein level of CD3δ in cells, probably depending on its weak deubiquitinating activity and the Ub-binding properties of the UBA domains. Thus, the non-activating catalysis of USP13 for K63-polyUb chains implies that it may function differently from USP5 in cellular deubiquitination processes.
PubMed: 22216260
DOI: 10.1371/journal.pone.0029362
主引用文献が同じPDBエントリー
実験手法
SOLUTION NMR
構造検証レポート
Validation report summary of 2lbc
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-01-28に公開中

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