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Crystal structure of DeSI-1, a novel deSUMOylase belonging to a putative isopeptidase superfamily
- Crystal structure of DeSI-1, a novel deSUMOylase belonging to a putative isopeptidase superfamily
- Suh H.-Y.; Kim J.-H.; Woo J.-S.; Ku B.; Shin E.J.; Yun Y.; Oh B.-H.
- Ewha Authors
- SCOPUS Author ID
- Issue Date
- Journal Title
- Proteins: Structure, Function and Bioinformatics
- vol. 80, no. 8, pp. 2099 - 2104
- SCI; SCIE; 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. © 2012 Wiley Periodicals, Inc.
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