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

Title
Crystal structure of DeSI-1, a novel deSUMOylase belonging to a putative isopeptidase superfamily
Authors
Suh H.-Y.Kim J.-H.Woo J.-S.Ku B.Shin E.J.Yun Y.Oh B.-H.
Ewha Authors
윤영대
SCOPUS Author ID
윤영대scopus
Issue Date
2012
Journal Title
Proteins: Structure, Function and Bioinformatics
ISSN
0887-3585JCR Link
Citation
vol. 80, no. 8, pp. 2099 - 2104
Indexed
SCI; SCIE; SCOPUS WOS scopus
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. © 2012 Wiley Periodicals, Inc.
DOI
10.1002/prot.24093
Appears in Collections:
자연과학대학 > 생명과학전공 > Journal papers
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