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TitleUnravelling the Specificity of Laminaribiose Phosphorylase from Paenibacillus sp. YM-1 towards Donor Substrates Glucose/Mannose 1-Phosphate by Using X-ray Crystallography and Saturation Transfer Difference NMR Spectroscopy.
Journal, issue, pagesChembiochem, Vol. 20, Page 181-192, Year 2019
Publish dateMay 4, 2018 (structure data deposition date)
AuthorsKuhaudomlarp, S. / Walpole, S. / Stevenson, C.E.M. / Nepogodiev, S.A. / Lawson, D.M. / Angulo, J. / Field, R.A.
External linksChembiochem / PubMed:29856496
MethodsX-ray diffraction
Resolution1.82 - 2.5 Å
Structure data

PDB-6ggy:
Paenibacillus sp. YM1 laminaribiose phosphorylase with sulphate bound
Method: X-RAY DIFFRACTION / Resolution: 1.95 Å

PDB-6gh2:
Paenibacillus sp. YM1 laminaribiose phosphorylase with alpha-glc-1-phosphate bound
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-6gh3:
Paenibacillus sp. YM1 laminaribiose phosphorylase with alpha-man-1-phosphate bound
Method: X-RAY DIFFRACTION / Resolution: 1.82 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-G1P:
1-O-phosphono-alpha-D-glucopyranose

ChemComp-M1P:
1-O-phosphono-alpha-D-mannopyranose

Source
  • paenibacillus sp. ym1 (bacteria)
KeywordsHYDROLASE / laminaribiose phosphorylase / Glycosyl hydrolase 94 / disaccharide synthesis / CARBOHYDRATE

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