3UEL

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

Summary for 3UEL

• Entry DOI: 10.2210/pdb3uel/pdb
• Related: 3UEK
• Descriptor: Poly(ADP-ribose) glycohydrolase, 5'-O-[(S)-{[(S)-{[(2R,3R,4S)-3,4-DIHYDROXYPYRROLIDIN-2-YL]METHOXY}(HYDROXY)PHOSPHORYL]OXY}(HYDROXY)PHOSPHORYL]ADENOSINE (2 entities in total)
• Functional Keywords: mammalian parg, macrodomain, adp-hpd, hydrolase
• Biological source: Rattus norvegicus (brown rat,rat,rats)
• Cellular location: Nucleus (By similarity): Q9QYM2
• Total number of polymer chains: 3
• Total formula weight: 204967.46

Authors

Kim, I.K.,Kiefer, J.R.,Stegemann, R.A.,Classen, S.,Tainer, J.A.,Ellenberger, T. (deposition date: 2011-10-30, release date: 2012-05-23, Last modification date: 2024-02-28)

Primary citation

Kim, I.K.,Kiefer, J.R.,Ho, C.M.,Stegeman, R.A.,Classen, S.,Tainer, J.A.,Ellenberger, T.
Structure of mammalian poly(ADP-ribose) glycohydrolase reveals a flexible tyrosine clasp as a substrate-binding element.
Nat.Struct.Mol.Biol., 19:653-656, 2012

PubMed Abstract: 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.

PubMed: 22609859
DOI: 10.1038/nsmb.2305

Experimental method

X-RAY DIFFRACTION (3 Å)