Crystal structure of the Ube2K/E2-25K and K48-linked di-ubiquitin complex provides structural insight into the mechanism of K48-specific ubiquitin chain synthesis

2018 ◽  
Vol 506 (1) ◽  
pp. 102-107 ◽  
Author(s):  
Jung-Gyu Lee ◽  
Hyung-Seop Youn ◽  
Jung Youn Kang ◽  
Sam-Yong Park ◽  
Akinori Kidera ◽  
...  
2016 ◽  
Vol 105 (8) ◽  
pp. 2298-2301
Author(s):  
Yukio Morimoto ◽  
Hideko Nagasawa ◽  
Yoshihiro Uto ◽  
Toshiyuki Chatake ◽  
Hitoshi Hori

2005 ◽  
Vol 348 (5) ◽  
pp. 1139-1151 ◽  
Author(s):  
Rosmarie Friemann ◽  
Maja M. Ivkovic-Jensen ◽  
Daniel J. Lessner ◽  
Chi-Li Yu ◽  
David T. Gibson ◽  
...  

2014 ◽  
Vol 112 (1) ◽  
pp. 106-111 ◽  
Author(s):  
Jee-Young Mock ◽  
Justin William Chartron ◽  
Ma’ayan Zaslaver ◽  
Yue Xu ◽  
Yihong Ye ◽  
...  

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.


2020 ◽  
Vol 150 ◽  
pp. 1272-1280
Author(s):  
Priya Rani ◽  
Gunjan Gautam ◽  
Tamanna Anwar ◽  
Samudrala Gourinath ◽  
Asis Datta

2003 ◽  
Vol 185 (14) ◽  
pp. 4276-4279 ◽  
Author(s):  
Rita Berisio ◽  
Joerg Harms ◽  
Frank Schluenzen ◽  
Raz Zarivach ◽  
Harly A. S. Hansen ◽  
...  

ABSTRACT The crystal structure of the ketolide telithromycin bound to the Deinococcus radiodurans large ribosomal subunit shows that telithromycin blocks the ribosomal exit tunnel and interacts with domains II and V of the 23S RNA. Comparisons to other clinically relevant macrolides provided structural insights into its enhanced activity against macrolide-resistant strains.


2006 ◽  
Vol 360 (5) ◽  
pp. 946-955 ◽  
Author(s):  
Dae Gwin Jeong ◽  
Tae-Sung Yoon ◽  
Jae Hoon Kim ◽  
Mi Young Shim ◽  
Suk-Kyeong Jung ◽  
...  

2021 ◽  
Vol 22 (8) ◽  
pp. 3812
Author(s):  
Jin Wang ◽  
Lei Li ◽  
Zhenhua Ming ◽  
Lijie Wu ◽  
Liming Yan

Tubules of the endoplasmic reticulum (ER) spread into the buds of yeast by an actin-based mechanism and, upon entry, become attached to the polarisome, a proteinaceous micro-compartment below the tip of the bud. The minimal tether between polarisome and cortical ER is formed by a protein complex consisting of Epo1, a member of the polarisome, Scs2, a membrane protein of the ER and Cdc42 guanosine triphosphatase-activating protein Bem3. Here, we report the crystal structure of a complex between Epo1 and Bem3. In addition, we characterize through the hydrogen/deuterium (H/D) exchange assay the interface between Scs2 and Epo1. Our findings provide a first structural insight into the molecular architecture of the link between cortical ER and the polarisome.


2014 ◽  
Vol 42 (6) ◽  
pp. 4113-4122 ◽  
Author(s):  
Dmitrij Golovenko ◽  
Elena Manakova ◽  
Linas Zakrys ◽  
Mindaugas Zaremba ◽  
Giedrius Sasnauskas ◽  
...  

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