HHARI in motion reveals an unexpected substrate recognition site for RBR ligases

Capturing the enzymatic activity of RBR ligases in molecular detail is challenging due to their inherent dynamic behavior. In this issue of Structure, Reiter and colleagues tackle this problem using a multidisciplinary approach. They show that activation of the ubiquitin ligase HHARI by phosphorylation induces a major conformational rearrangement, which reveals an unexpected substrate binding site.

Automated summary

In this study, a multidisciplinary approach was used to investigate the enzymatic activity of RBR ligases, revealing an unexpected substrate binding site.