2WP7

Crystal structure of deSUMOylase(DUF862)

Summary for 2WP7

• Entry DOI: 10.2210/pdb2wp7/pdb
• Descriptor: PPPDE PEPTIDASE DOMAIN-CONTAINING PROTEIN 2 (2 entities in total)
• Functional Keywords: hydrolase, phosphoprotein, ubiquitin-like protein
• Biological source: MUS MUSCULUS (MOUSE)
• Cellular location: Cytoplasm: Q9CQT7
• Total number of polymer chains: 1
• Total formula weight: 18398.68

Authors

Kim, J.H.,Woo, J.S.,Oh, B.H. (deposition date: 2009-08-03, release date: 2010-09-01, Last modification date: 2023-12-20)

Primary citation

Suh, H.Y.,Kim, J.H.,Woo, J.S.,Ku, B.,Shin, E.J.,Yun, Y.,Oh, B.H.
Crystal Structure of Desi-1, a Novel Desumoylase Belonging to a Putative Isopeptidase Superfamily.
Proteins, 80:2099-, 2012

PubMed 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.

PubMed: 22498933
DOI: 10.1002/PROT.24093

Experimental method

X-RAY DIFFRACTION (1.9 Å)