3uel

Crystal structure of the catalytic domain of rat poly (ADP-ribose) glycohydrolase bound to ADP-HPDCrystal structure of the catalytic domain of rat poly (ADP-ribose) glycohydrolase bound to ADP-HPD

Structural highlights 3uel is a 3 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: Related: 3uek Gene: Parg (Rattus norvegicus) Activity: Poly(ADP-ribose) glycohydrolase, with EC number 3.2.1.143 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Reversible post-translational modification by poly(ADP-ribose) (PAR) regulates chromatin structure, DNA repair and cell fate in response to genotoxic stress. PAR glycohydrolase (PARG) removes PAR chains from poly ADP-ribosylated proteins to restore protein function and release oligo(ADP-ribose) chains to signal damage. Here we report crystal structures of mammalian PARG and its complex with a substrate mimic that reveal an open substrate-binding site and a unique 'tyrosine clasp' enabling endoglycosidic cleavage of branched PAR chains. Structure of mammalian poly(ADP-ribose) glycohydrolase reveals a flexible tyrosine clasp as a substrate-binding element.,Kim IK, Kiefer JR, Ho CM, Stegeman RA, Classen S, Tainer JA, Ellenberger T Nat Struct Mol Biol. 2012 May 20;19(6):653-6. doi: 10.1038/nsmb.2305. PMID:22609859 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 3uel, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image