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Active site remodelling accompanies thioester bond formation in the SUMO E1
The post-translational modification of cellular proteins by ubiquitin (Ub) and ubiquitin-like (Ubl) proteins — such as SUMO — regulates a broad array of cellular processes. E1 enzymes activate Ub and Ubl in two steps, by carboxy-terminal adenylation and thioester bond formation to a catalytic cysteine, but the structural basis for the intermediates remains unknown. Crystal structures for SUMO E1 in complex with SUMO adenylate and tetrahedral intermediate analogues are now reported and analysed.
- Shaun K. Olsen
- , Allan D. Capili
- & Christopher D. Lima