3M63

Crystal structure of Ufd2 in complex with the ubiquitin-like (UBL) domain of Dsk2

3M63 の概要

• エントリーDOI: 10.2210/pdb3m63/pdb
• 関連するPDBエントリー: 3M62
• 分子名称: Ubiquitin conjugation factor E4, Ubiquitin domain-containing protein DSK2, PENTAETHYLENE GLYCOL, ... (5 entities in total)
• 機能のキーワード: armadillo-like repeats, ubl conjugation pathway, nucleus, phosphoprotein, ligase-protein binding complex, ligase/protein binding
• 由来する生物種: Saccharomyces cerevisiae (yeast); 詳細
• 細胞内の位置: Cytoplasm: P54860; Nucleus (Probable): P48510
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 122623.66

構造登録者

Haenzelmann, P.,Schindelin, H. (登録日: 2010-03-15, 公開日: 2010-04-28, 最終更新日: 2023-09-06)

主引用文献

Hanzelmann, P.,Stingele, J.,Hofmann, K.,Schindelin, H.,Raasi, S.
The yeast E4 ubiquitin ligase Ufd2 interacts with the ubiquitin-like domains of Rad23 and Dsk2 via a novel and distinct ubiquitin-like binding domain.
J.Biol.Chem., 285:20390-20398, 2010

PubMed Abstract: Proteins containing ubiquitin-like (UBL) and ubiquitin-associated (UBA) domains interact with various binding partners and function as hubs during ubiquitin-mediated protein degradation. A common interaction of the budding yeast UBL-UBA proteins Rad23 and Dsk2 with the E4 ubiquitin ligase Ufd2 has been described in endoplasmic reticulum-associated degradation among other pathways. The UBL domains of Rad23 and Dsk2 play a prominent role in this process by interacting with Ufd2 and different subunits of the 26 S proteasome. Here, we report crystal structures of Ufd2 in complex with the UBL domains of Rad23 and Dsk2. The N-terminal UBL-interacting region of Ufd2 exhibits a unique sequence pattern, which is distinct from any known ubiquitin- or UBL-binding domain identified so far. Residue-specific differences exist in the interactions of these UBL domains with Ufd2, which are coupled to subtle differences in their binding affinities. The molecular details of their differential interactions point to a role for adaptive evolution in shaping these interfaces.

PubMed: 20427284
DOI: 10.1074/jbc.M110.112532

実験手法

X-RAY DIFFRACTION (2.4 Å)