4WWR

Crystal Structure of Bag6-Ubl4A Dimerization Domain

Summary for 4WWR

• Entry DOI: 10.2210/pdb4wwr/pdb
• Descriptor: Ubiquitin-like protein 4A, Large proline-rich protein BAG6 (3 entities in total)
• Functional Keywords: endoplasmic reticulum, recombinant proteins, human, transport protein
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 8
• Total formula weight: 45739.72

Authors

Mock, J.Y.,Chartron, J.W.,Clemons Jr., W.M. (deposition date: 2014-11-12, release date: 2014-12-24, Last modification date: 2023-12-27)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2 Å)