8DAT

Saccharomyces cerevisiae Ufd1/Npl4/Cdc48 complex bound to three ubiquitin moieties in presence of SUMO-ubiquitin(K48polyUb)-mEOS and ATP, state 1 (intB)

8DAT の概要

• エントリーDOI: 10.2210/pdb8dat/pdb
• EMDBエントリー: 27275
• 分子名称: Cell division control protein 48, Nuclear protein localization protein 4, Ubiquitin fusion degradation protein 1, ... (7 entities in total)
• 機能のキーワード: atpase, atpase complex, ubiquitin, sumo, smt3, quality control, motor protein
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast); 詳細
• タンパク質・核酸の鎖数: 11
• 化学式量合計: 691844.39

構造登録者

Lee, H.G.,Lima, C.D. (登録日: 2022-06-14, 公開日: 2022-11-30, 最終更新日: 2024-10-30)

主引用文献

Lee, H.G.,Lemmon, A.A.,Lima, C.D.
SUMO enhances unfolding of SUMO-polyubiquitin-modified substrates by the Ufd1/Npl4/Cdc48 complex.
Proc.Natl.Acad.Sci.USA, 120:e2213703120-e2213703120, 2023

PubMed Abstract: The Ufd1/Npl4/Cdc48 complex is a universal protein segregase that plays key roles in eukaryotic cellular processes. Its functions orchestrating the clearance or removal of polyubiquitylated targets are established; however, prior studies suggest that the complex also targets substrates modified by the ubiquitin-like protein SUMO. Here, we show that interactions between Ufd1 and SUMO enhance unfolding of substrates modified by SUMO-polyubiquitin hybrid chains by the budding yeast Ufd1/Npl4/Cdc48 complex compared to substrates modified by polyubiquitin chains, a difference that is accentuated when the complex has a choice between these substrates. Incubating Ufd1/Npl4/Cdc48 with a substrate modified by a SUMO-polyubiquitin hybrid chain produced a series of single-particle cryo-EM structures that reveal features of interactions between Ufd1/Npl4/Cdc48 and ubiquitin prior to and during unfolding of ubiquitin. These results are consistent with cellular functions for SUMO and ubiquitin modifications and support a physical model wherein Ufd1/Npl4/Cdc48, SUMO, and ubiquitin conjugation pathways converge to promote clearance of proteins modified with SUMO and polyubiquitin.

PubMed: 36574706
DOI: 10.1073/pnas.2213703120

実験手法

ELECTRON MICROSCOPY (3.8 Å)