title: Crystal structure of DeSI-1, a novel deSUMOylase belonging to a putative isopeptidase superfamily.
abstract: 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.
authors.affiliation: Department of Biological Sciences, KAIST Institute for the Biocentury, Korea Advanced Institute of Science and Technology, Daejeon, Korea.
authors.forename: Hye-Young
authors.initials: HY
authors.lastname: Suh
authors.forename: Ji-Hoon
authors.initials: JH
authors.lastname: Kim
authors.forename: Jae-Sung
authors.initials: JS
authors.lastname: Woo
authors.forename: Bonsu
authors.initials: B
authors.lastname: Ku
authors.forename: Eun Ju
authors.initials: EJ
authors.lastname: Shin
authors.forename: Yungdae
authors.initials: Y
authors.lastname: Yun
authors.forename: Byung-Ha
authors.initials: BH
authors.lastname: Oh
mesh_terms: D000818:Animals; D019759:Carbon-Nitrogen Lyases / Q000737:chemistry*; D002384:Catalysis; D020134:Catalytic Domain; D017124:Conserved Sequence; D003460:Crystallization; D003545:Cysteine / Q000737:chemistry*; D006639:Histidine / Q000737:chemistry*; D051379:Mice; D011487:Protein Conformation
chemical_list: D006639:Histidine; D019759:Carbon-Nitrogen Lyases; C574164:deSumoylating Isopeptidase 1, mouse; D003545:Cysteine