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Structure paper

TitleStructure and mechanism of a canonical poly(ADP-ribose) glycohydrolase.
Journal, issue, pagesNat Commun, Vol. 3, Page 878-878, Year 2012
Publish dateApr 17, 2012 (structure data deposition date)
AuthorsDunstan, M.S. / Barkauskaite, E. / Lafite, P. / Knezevic, C.E. / Brassington, A. / Ahel, M. / Hergenrother, P.J. / Leys, D. / Ahel, I.
External linksNat Commun / PubMed:22673905
MethodsX-ray diffraction
Resolution1.95 - 2.399 Å
Structure data

PDB-4epp:
Canonical poly(ADP-ribose) glycohydrolase from Tetrahymena thermophila.
Method: X-RAY DIFFRACTION / Resolution: 1.95 Å

PDB-4epq:
canonical poly(ADP-ribose) glycohydrolase RBPI inhibitor complex from Tetrahymena thermophila
Method: X-RAY DIFFRACTION / Resolution: 2.399 Å

Chemicals

ChemComp-APR:
ADENOSINE-5-DIPHOSPHORIBOSE

ChemComp-HOH:
WATER

ChemComp-0RR:
3-{(5Z)-5-[5-chloro-1-(2,6-dichlorobenzyl)-2-oxo-1,2-dihydro-3H-indol-3-ylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl}propanoic acid

Source
  • tetrahymena thermophila (eukaryote)
KeywordsHYDROLASE / Marco domain / PAR / HYDROLASE/INHIBITOR / Macro domain / HYDROLASE-INHIBITOR complex

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