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TitleVisualization of poly(ADP-ribose) bound to PARG reveals inherent balance between exo- and endo-glycohydrolase activities.
Journal, issue, pagesNat Commun, Vol. 4, Page 2164-2164, Year 2013
Publish dateJun 4, 2013 (structure data deposition date)
AuthorsBarkauskaite, E. / Brassington, A. / Tan, E.S. / Warwicker, J. / Dunstan, M.S. / Banos, B. / Lafite, P. / Ahel, M. / Mitchison, T.J. / Ahel, I. / Leys, D.
External linksNat Commun / PubMed:23917065
MethodsX-ray diffraction
Resolution1.46 Å
Structure data

PDB-4l2h:
Structure of a catalytically inactive PARG in complex with a poly-ADP-ribose fragment
Method: X-RAY DIFFRACTION / Resolution: 1.46 Å

Chemicals

ChemComp-AR6:
[(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-DIHYDROXY-OXOLAN-2-YL]METHYL

ChemComp-HOH:
WATER

Source
  • tetrahymena thermophila (eukaryote)
KeywordsHYDROLASE / macrodomain / poly-ADP-ribose glycohydrolase / poly-ADP-ribose

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