6EI1

Crystal structure of the covalent complex between deubiquitinase ZUFSP (ZUP1) and Ubiquitin-PA

6EI1 の概要

• エントリーDOI: 10.2210/pdb6ei1/pdb
• 分子名称: Zinc finger with UFM1-specific peptidase domain protein, Polyubiquitin-B, prop-2-en-1-amine, ... (6 entities in total)
• 機能のキーワード: k63, ubiquitin, deubiquitinase, cysteine peptidase, hydrolase, zup1
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 48506.36

構造登録者

Pichlo, C.,Baumann, U.,Hofmann, K.,Hermanns, T. (登録日: 2017-09-16, 公開日: 2018-03-07, 最終更新日: 2025-04-09)

主引用文献

Hermanns, T.,Pichlo, C.,Woiwode, I.,Klopffleisch, K.,Witting, K.F.,Ovaa, H.,Baumann, U.,Hofmann, K.
A family of unconventional deubiquitinases with modular chain specificity determinants.
Nat Commun, 9:799-799, 2018

PubMed Abstract: Deubiquitinating enzymes (DUBs) regulate ubiquitin signaling by trimming ubiquitin chains or removing ubiquitin from modified substrates. Similar activities exist for ubiquitin-related modifiers, although the enzymes involved are usually not related. Here, we report human ZUFSP (also known as ZUP1 and C6orf113) and fission yeast Mug105 as founding members of a DUB family different from the six known DUB classes. The crystal structure of human ZUFSP in covalent complex with propargylated ubiquitin shows that the DUB family shares a fold with UFM1- and Atg8-specific proteases, but uses a different active site more similar to canonical DUB enzymes. ZUFSP family members differ widely in linkage specificity through differential use of modular ubiquitin-binding domains (UBDs). While the minimalistic Mug105 prefers K48 chains, ZUFSP uses multiple UBDs for its K63-specific endo-DUB activity. K63 specificity, localization, and protein interaction network suggest a role for ZUFSP in DNA damage response.

PubMed: 29476094
DOI: 10.1038/s41467-018-03148-5

実験手法

X-RAY DIFFRACTION (1.732 Å)