Crystal structure of DeSI-1, a novel deSUMOylase belonging to a putative isopeptidase superfamily

Hye Young Suh, Ji Hoon Kim, Jae Sung Woo, Bonsu Ku, Eun Ju Shin, Yungdae Yun, Byung Ha Oh

Research output: Contribution to journalArticle

17 Citations (Scopus)


Post-translational modification by small ubiquitin-like modifier (SUMO) can be reversed by sentrin/SUMO-specific proteases (SENPs), the first known class of deSUMOylase. Recently, we identified a new deSUMOylating enzyme DeSI-1, which is distinct from SENPs and belongs to the putative deubiquitinating isopeptidase PPPDE superfamily. Herein, we report the crystal structure of DeSI-1, revealing that this enzyme forms a homodimer and that the groove between the two subunits is the active site harboring two absolutely conserved cysteine and histidine residues that form a catalytic dyad. We also show that DeSI-1 exhibits an extremely low endopeptidase activity toward precursor forms of SUMO-1 and SUMO-2, unlike SENPs.

Original languageEnglish
Pages (from-to)2099-2104
Number of pages6
JournalProteins: Structure, Function and Bioinformatics
Issue number8
Publication statusPublished - 2012 Aug 1
Externally publishedYes



  • DeSI-1
  • DeSUMOylase
  • SUMO
  • Structure
  • Ubiquitin-like protein

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Biology

Cite this