Details

Autor(en) / Beteiligte

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

Titel

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

Ist Teil von

• Proteins, structure, function, and bioinformatics, 2012-08, Vol.80 (8), p.2099-2104

Ort / Verlag

Hoboken: Wiley Subscription Services, Inc., A Wiley Company

Erscheinungsjahr

2012

Quelle

Wiley-Blackwell Journals

Beschreibungen/Notizen

• 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. Proteins 2012. © 2012 Wiley Periodicals, Inc.