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TitleGlycogen phosphorylase revisited: extending the resolution of the R- and T-state structures of the free enzyme and in complex with allosteric activators.
Journal, issue, pagesActa Crystallogr. ,Sect. F, Vol. 77, Page 303-311, Year 2021
Publish dateAug 7, 2008 (structure data deposition date)
AuthorsLeonidas, D.D. / Zographos, S.E. / Tsitsanou, K.E. / Skamnaki, V.T. / Stravodimos, G. / Kyriakis, E.
External linksActa Crystallogr. ,Sect. F / PubMed:34473107
MethodsX-ray diffraction
Resolution1.45 - 2.7 Å
Structure data

PDB-3e3l:
The R-state Glycogen Phosphorylase
Method: X-RAY DIFFRACTION / Resolution: 2.59 Å

PDB-3e3n:
The Glycogen phosphorylase b R state- AMP complex
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

PDB-3e3o:
Glycogen phosphorylase R state-IMP complex
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

PDB-7p7d:
Rabbit muscle Glycogen Phosphorylase T state
Method: X-RAY DIFFRACTION / Resolution: 1.45 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

ChemComp-AMP:
ADENOSINE MONOPHOSPHATE / AMP*YM

ChemComp-IMP:
INOSINIC ACID

ChemComp-DMS:
DIMETHYL SULFOXIDE / DMSO, precipitant*YM

Source
  • oryctolagus cuniculus (rabbit)
KeywordsTRANSFERASE / GLYCOGENOLYSIS / INHIBITION / TYPE 2 DIABETES / Allosteric enzyme / Carbohydrate metabolism / Glycogen metabolism / Glycosyltransferase / Nucleotide-binding / Phosphoprotein / Pyridoxal phosphate

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