Structural Diversity of Ubiquitin E3 Ligase

The post-translational modification of proteins regulates many biological processes. Their dysfunction relates to diseases. Ubiquitination is one of the post-translational modifications that target lysine residue and regulate many cellular processes. Three enzymes are required for achieving the ubiquitination reaction: ubiquitin-activating enzyme (E1), ubiquitin-conjugating enzyme (E2), and ubiquitin ligase (E3). E3s play a pivotal role in selecting substrates. Many structural studies have been conducted to reveal the molecular mechanism of the ubiquitination reaction. Recently, the structure of PCAF_N, a newly categorized E3 ligase, was reported. We present a review of the recent progress toward the structural understanding of E3 ligases.

Automated summary

Post-translational modifications of proteins play a critical role in regulating biological processes and their dysfunction can be linked to diseases. Ubiquitination, a type of post-translational modification, involves a complex reaction requiring three enzymes. Recent studies have focused on the structural understanding of E3 ligases, with advancements such as the characterization of PCAF_N, a newly categorized E3 ligase.