A CBM20 low-affinity starch-binding domain from glucan, water dikinase

Camilla Christiansen, Maher Abou Hachem, M.A. Glaring, A. Vikso-Nielsen, B.W. Sigurskjold, Birte Svensson, A. Blennow

    Research output: Contribution to journalJournal articleResearchpeer-review


    The family 20 carbohydrate-binding module (CBM20) of the Arabidopsis starch phosphorylator glucan, water dikinase 3 (GWD3) was heterologously produced and its properties were compared to the CBM20 from a fungal glucoamylase (GA). The GWD3 CBM20 has 50-fold lower affinity for cyclodextrins than that from GA. Homology modelling identified possible structural elements responsible for this weak binding of the intracellular CBM20. Differential binding of fluorescein-labelled GWD3 and GA modules to starch granules in vitro was demonstrated by confocal laser scanning microscopy and yellow fluorescent protein-tagged GWD3 CBM20 expressed in tobacco confirmed binding to starch granules in planta.
    Original languageEnglish
    JournalFEBS Letters
    Issue number7
    Pages (from-to)1159-1163
    Publication statusPublished - 2009


    • Carbohydrate-binding module 20
    • Starch-binding domain
    • Surface plasmon resonance
    • Glucan, water dikinase
    • Bioimaging


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