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Structure paper

TitlePhosphorylase Recognition and Phosphorylysis of its Oligosaccharide Substrate: Answers to a Long Outstanding Question
Journal, issue, pagesEmbo J., Vol. 18, Page 4619-, Year 1999
Publish dateJul 11, 2000 (structure data deposition date)
AuthorsWatson, K.A. / Mccleverty, C. / Geremia, S. / Cottaz, S. / Driguez, H. / Johnson, L.N.
External linksEmbo J. / PubMed:10469642
MethodsX-ray diffraction
Resolution2 - 2.9 Å
Structure data

PDB-1e4o:
Phosphorylase recognition and phosphorolysis of its oligosaccharide substrate: answers to a long outstanding question
Method: X-RAY DIFFRACTION / Resolution: 2.9 Å

PDB-1qm5:
Phosphorylase recognition and phosphorylysis of its oligosaccharide substrate: answers to a long outstanding question
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-PLP:
PYRIDOXAL-5'-PHOSPHATE

ChemComp-HOH:
WATER

ChemComp-PO4:
PHOSPHATE ION

ChemComp-GLC:
alpha-D-glucopyranose

Source
  • escherichia coli (E. coli)
KeywordsHYDROLASE / MALTOPENTAOSE / CARBOHYDRATE RECOGNITION / PHOSPHORYLASE / BINARY AND TERNARY OLIGOSACCHARIDE COMPLEXES / THIO-OLIGOSACCHARIDE / PHOSPHOROLYSIS / MALP / GLYCOSYLTRANSFERASE

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