Structural insights into E1 recognition and the ubiquitin-conjugating activity of the E2 enzyme Cdc34
The E2 enzyme Cdc34 plays a critical role in cell cycle progression but the structural bases for its activities are unknown. Here, the authors present crystal structures of Cdc34 alone, in complex with E1, and in complex with Ub that provide insights into the mechanism of Cdc34 activity in the cell.
Guardado en:
Autores principales: | Katelyn M. Williams, Shuo Qie, James H. Atkison, Sabrina Salazar-Arango, J. Alan Diehl, Shaun K. Olsen |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2019
|
Materias: | |
Acceso en línea: | https://doaj.org/article/34fe16ea76e54aafba4e3a93fe290c25 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Structural insights into the mechanism and E2 specificity of the RBR E3 ubiquitin ligase HHARI
por: Lingmin Yuan, et al.
Publicado: (2017) -
Genome-wide identification and expression analysis of E2 ubiquitin-conjugating enzymes in tomato
por: Bhaskar Sharma, et al.
Publicado: (2017) -
Molecular mechanism of a covalent allosteric inhibitor of SUMO E1 activating enzyme
por: Zongyang Lv, et al.
Publicado: (2018) -
African swine fever virus encodes for an E2-ubiquitin conjugating enzyme that is mono- and di-ubiquitinated and required for viral replication cycle
por: Ferdinando B. Freitas, et al.
Publicado: (2018) -
miR-543 impairs breast cancer cell phenotypes by targeting and suppressing ubiquitin-conjugating enzyme E2T (UBE2T)
por: Li Li, et al.
Publicado: (2021)