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 Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, RCSB, PDBsum 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.

Proteopedia Page Contributors and Editors (what is this?)

OCA