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.
Saved in:
| Main Authors: | , , , , , |
|---|---|
| Format: | article |
| Language: | EN |
| Published: |
Nature Portfolio
2019
|
| Subjects: | |
| Online Access: | https://doaj.org/article/34fe16ea76e54aafba4e3a93fe290c25 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| Summary: | 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. |
|---|