7OY3

Crystal structure of depupylase Dop in complex with phosphorylated Pup and ADP

7OY3 の概要

• エントリーDOI: 10.2210/pdb7oy3/pdb
• 分子名称: Depupylase, Prokaryotic ubiquitin-like protein Pup, POTASSIUM ION, ... (10 entities in total)
• 機能のキーワード: depupylase, atp hydrolysis, deamidase, phosphorylated pup binding, hydrolase
• 由来する生物種: Acidothermus cellulolyticus; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 61953.54

構造登録者

Cui, H. (登録日: 2021-06-23, 公開日: 2021-12-01, 最終更新日: 2024-02-07)

主引用文献

Cui, H.,Muller, A.U.,Leibundgut, M.,Tian, J.,Ban, N.,Weber-Ban, E.
Structures of prokaryotic ubiquitin-like protein Pup in complex with depupylase Dop reveal the mechanism of catalytic phosphate formation.
Nat Commun, 12:6635-6635, 2021

PubMed Abstract: Pupylation is the post-translational modification of lysine side chains with prokaryotic ubiquitin-like protein (Pup) that targets proteins for proteasomal degradation in mycobacteria and other members of Actinobacteria. Pup ligase PafA and depupylase Dop are the two enzymes acting in this pathway. Although they share close structural and sequence homology indicative of a common evolutionary origin, they catalyze opposing reactions. Here, we report a series of high-resolution crystal structures of Dop in different functional states along the reaction pathway, including Pup-bound states in distinct conformations. In combination with biochemical analysis, the structures explain the role of the C-terminal residue of Pup in ATP hydrolysis, the process that generates the catalytic phosphate in the active site, and suggest a role for the Dop-loop as an allosteric sensor for Pup-binding and ATP cleavage.

PubMed: 34789727
DOI: 10.1038/s41467-021-26848-x

実験手法

X-RAY DIFFRACTION (1.78 Å)