4WWR

Crystal Structure of Bag6-Ubl4A Dimerization Domain

4WWR の概要

• エントリーDOI: 10.2210/pdb4wwr/pdb
• 分子名称: Ubiquitin-like protein 4A, Large proline-rich protein BAG6 (3 entities in total)
• 機能のキーワード: endoplasmic reticulum, recombinant proteins, human, transport protein
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 45739.72

構造登録者

Mock, J.Y.,Chartron, J.W.,Clemons Jr., W.M. (登録日: 2014-11-12, 公開日: 2014-12-24, 最終更新日: 2023-12-27)

主引用文献

Mock, J.Y.,Chartron, J.W.,Zaslaver, M.,Xu, Y.,Ye, Y.,Clemons, W.M.
Bag6 complex contains a minimal tail-anchor-targeting module and a mock BAG domain.
Proc.Natl.Acad.Sci.USA, 112:106-111, 2015

PubMed Abstract: BCL2-associated athanogene cochaperone 6 (Bag6) plays a central role in cellular homeostasis in a diverse array of processes and is part of the heterotrimeric Bag6 complex, which also includes ubiquitin-like 4A (Ubl4A) and transmembrane domain recognition complex 35 (TRC35). This complex recently has been shown to be important in the TRC pathway, the mislocalized protein degradation pathway, and the endoplasmic reticulum-associated degradation pathway. Here we define the architecture of the Bag6 complex, demonstrating that both TRC35 and Ubl4A have distinct C-terminal binding sites on Bag6 defining a minimal Bag6 complex. A crystal structure of the Bag6-Ubl4A dimer demonstrates that Bag6-BAG is not a canonical BAG domain, and this finding is substantiated biochemically. Remarkably, the minimal Bag6 complex defined here facilitates tail-anchored substrate transfer from small glutamine-rich tetratricopeptide repeat-containing protein α to TRC40. These findings provide structural insight into the complex network of proteins coordinated by Bag6.

PubMed: 25535373
DOI: 10.1073/pnas.1402745112

実験手法

X-RAY DIFFRACTION (2 Å)