3ZRH

Crystal structure of the Lys29, Lys33-linkage-specific TRABID OTU deubiquitinase domain reveals an Ankyrin-repeat ubiquitin binding domain (AnkUBD)

3ZRH の概要

• エントリーDOI: 10.2210/pdb3zrh/pdb
• 分子名称: UBIQUITIN THIOESTERASE ZRANB1, 1,2-ETHANEDIOL, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: hydrolase, deubiquitinating enzyme, wnt signaling, ovarian tumor domain
• 由来する生物種: HOMO SAPIENS (HUMAN)
• 細胞内の位置: Cytoplasm: Q9UGI0
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 52544.15

構造登録者

Licchesi, J.D.F.,Akutsu, M.,Komander, D. (登録日: 2011-06-16, 公開日: 2011-12-14, 最終更新日: 2024-05-08)

主引用文献

Licchesi, J.D.F.,Mieszczanek, J.,Mevissen, T.E.T.,Rutherford, T.J.,Akutsu, M.,Virdee, S.,Oualid, F.E.,Chin, J.W.,Ovaa, H.,Bienz, M.,Komander, D.
An Ankyrin-Repeat Ubiquitin-Binding Domain Determines Trabid'S Specificity for Atypical Ubiquitin Chains.
Nat.Struct.Mol.Biol., 19:62-, 2011

PubMed Abstract: Eight different types of ubiquitin linkages are present in eukaryotic cells that regulate diverse biological processes. Proteins that mediate specific assembly and disassembly of atypical Lys6, Lys27, Lys29 and Lys33 linkages are mainly unknown. We here reveal how the human ovarian tumor (OTU) domain deubiquitinase (DUB) TRABID specifically hydrolyzes both Lys29- and Lys33-linked diubiquitin. A crystal structure of the extended catalytic domain reveals an unpredicted ankyrin repeat domain that precedes an A20-like catalytic core. NMR analysis identifies the ankyrin domain as a new ubiquitin-binding fold, which we have termed AnkUBD, and DUB assays in vitro and in vivo show that this domain is crucial for TRABID efficiency and linkage specificity. Our data are consistent with AnkUBD functioning as an enzymatic S1' ubiquitin-binding site, which orients a ubiquitin chain so that Lys29 and Lys33 linkages are cleaved preferentially.

PubMed: 22157957
DOI: 10.1038/NSMB.2169

実験手法

X-RAY DIFFRACTION (2.23 Å)