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Structure paper

TitleDifferential catalytic promiscuity of the alkaline phosphatase superfamily bimetallo core reveals mechanistic features underlying enzyme evolution.
Journal, issue, pagesJ. Biol. Chem., Vol. 292, Page 20960-20974, Year 2017
Publish dateOct 18, 2016 (structure data deposition date)
AuthorsSunden, F. / AlSadhan, I. / Lyubimov, A. / Doukov, T. / Swan, J. / Herschlag, D.
External linksJ. Biol. Chem. / PubMed:29070681
MethodsX-ray diffraction
Resolution2.031 - 2.45 Å
Structure data

PDB-5too:
Crystal structure of alkaline phosphatase PafA T79S, N100A, K162A, R164A mutant
Method: X-RAY DIFFRACTION / Resolution: 2.031 Å

PDB-5tpq:
E. coli alkaline phosphatase D101A, D153A, R166S, E322A, K328A mutant
Method: X-RAY DIFFRACTION / Resolution: 2.45 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-PO4:
PHOSPHATE ION

Source
  • elizabethkingia meningoseptica (bacteria)
  • escherichia coli (strain k12) (bacteria)
KeywordsHYDROLASE / Alkaline Phosphatase / Phosphomonoesterase / PafA / Weak phosphate binder / Zinc bimetallo core / generalist enzyme / bimetallo motif / catalytic promiscuity / evolution / D101A/D153A/R166S/E322A/K328A

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