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TitleStructure of the Arabidopsis Glucan Phosphatase LIKE SEX FOUR2 Reveals a Unique Mechanism for Starch Dephosphorylation.
Journal, issue, pagesPlant Cell, Vol. 25, Page 2302-2314, Year 2013
Publish dateMay 29, 2013 (structure data deposition date)
AuthorsMeekins, D.A. / Guo, H.F. / Husodo, S. / Paasch, B.C. / Bridges, T.M. / Santelia, D. / Kotting, O. / Vander Kooi, C.W. / Gentry, M.S.
External linksPlant Cell / PubMed:23832589
MethodsX-ray diffraction
Resolution1.64 - 2.3 Å
Structure data

PDB-4kyq:
Structure of a product bound plant phosphatase
Method: X-RAY DIFFRACTION / Resolution: 1.64 Å

PDB-4kyr:
Structure of a product bound plant phosphatase
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

Chemicals

ChemComp-FLC:
CITRATE ANION

ChemComp-HOH:
WATER

ChemComp-PO4:
PHOSPHATE ION

Source
  • arabidopsis thaliana (thale cress)
KeywordsHYDROLASE / SUGAR BINDING PROTEIN / Dual Specificity Phosphatase (DSP) fold / Glucan (starch) phosphatase / Carbohydrate/Sugar Binding / chloroplast

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