2wp7 | pdb_00002wp7

Crystal structure of deSUMOylase(DUF862)

spinqualitylabelsall models 2wp7, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2wp7 is a 1 chain structure with sequence from Lk3 transgenic mice. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [DESI1_MOUSE] Protease which deconjugates SUMO1, SUMO2 and SUMO3 from some substrate proteins. Has isopeptidase but not SUMO-processing activity. Desumoylates ZBTB46. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Post-translational modification by SUMO can be reversed by 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 which 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. (c) 2012 Wiley-Liss, Inc. Crystal structure of DeSI-1, a novel deSUMOylase belonging to a putative isopeptidase superfamily.,Suh HY, Kim JH, Woo JS, Ku B, Shin EJ, Yun Y, Oh BH Proteins. 2012 Apr 13. doi: 10.1002/prot.24093. PMID:22498933 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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