Structure of mammalian poly(ADP-ribose) glycohydrolase reveals a flexible tyrosine clasp as a substrate-binding element.

In-Kwon Kim, James R Kiefer, Chris M W Ho, Roderick A Stegeman, Scott Classen, John A Tainer, Tom Ellenberger

Nature structural & molecular biology 2012 May 20

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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.

Citation

In-Kwon Kim, James R Kiefer, Chris M W Ho, Roderick A Stegeman, Scott Classen, John A Tainer, Tom Ellenberger. Structure of mammalian poly(ADP-ribose) glycohydrolase reveals a flexible tyrosine clasp as a substrate-binding element. Nature structural & molecular biology. 2012 May 20;19(6):653-6