4epp | pdb_00004epp

Canonical poly(ADP-ribose) glycohydrolase from Tetrahymena thermophila.

spinqualitylabelsall models 4epp, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4epp is a 2 chain structure with sequence from Tetrahymena thermophila. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: APR Related: 4epq Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Poly(ADP-ribosyl)ation is a reversible post-translational protein modification involved in the regulation of a number of cellular processes including DNA repair, chromatin structure, mitosis, transcription, checkpoint activation, apoptosis and asexual development. The reversion of poly(ADP-ribosyl)ation is catalysed by poly(ADP-ribose) (PAR) glycohydrolase (PARG), which specifically targets the unique PAR (1-2') ribose-ribose bonds. Here we report the structure and mechanism of the first canonical PARG from the protozoan Tetrahymena thermophila. In addition, we reveal the structure of T. thermophila PARG in a complex with a novel rhodanine-containing mammalian PARG inhibitor RBPI-3. Our data demonstrate that the protozoan PARG represents a good model for human PARG and is therefore likely to prove useful in guiding structure-based discovery of new classes of PARG inhibitors. Structure and mechanism of a canonical poly(ADP-ribose) glycohydrolase.,Dunstan MS, Barkauskaite E, Lafite P, Knezevic CE, Brassington A, Ahel M, Hergenrother PJ, Leys D, Ahel I Nat Commun. 2012 Jun 6;3:878. doi: 10.1038/ncomms1889. PMID:22673905 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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