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

    Abstract

    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
    Volume583
    Issue number7
    Pages (from-to)1159-1163
    ISSN0014-5793
    DOIs
    Publication statusPublished - 2009

    Keywords

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

    Cite this

    Christiansen, C., Abou Hachem, M., Glaring, M. A., Vikso-Nielsen, A., Sigurskjold, B. W., Svensson, B., & Blennow, A. (2009). A CBM20 low-affinity starch-binding domain from glucan, water dikinase. FEBS Letters, 583(7), 1159-1163. https://doi.org/10.1016/j.febslet.2009.02.045
    Christiansen, Camilla ; Abou Hachem, Maher ; Glaring, M.A. ; Vikso-Nielsen, A. ; Sigurskjold, B.W. ; Svensson, Birte ; Blennow, A. / A CBM20 low-affinity starch-binding domain from glucan, water dikinase. In: FEBS Letters. 2009 ; Vol. 583, No. 7. pp. 1159-1163.
    @article{7c6de35c899b42a087b4bc45b5b4987d,
    title = "A CBM20 low-affinity starch-binding domain from glucan, water dikinase",
    abstract = "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.",
    keywords = "Carbohydrate-binding module 20, Starch-binding domain, Surface plasmon resonance, Glucan, water dikinase, Bioimaging",
    author = "Camilla Christiansen and {Abou Hachem}, Maher and M.A. Glaring and A. Vikso-Nielsen and B.W. Sigurskjold and Birte Svensson and A. Blennow",
    year = "2009",
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    language = "English",
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    pages = "1159--1163",
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    Christiansen, C, Abou Hachem, M, Glaring, MA, Vikso-Nielsen, A, Sigurskjold, BW, Svensson, B & Blennow, A 2009, 'A CBM20 low-affinity starch-binding domain from glucan, water dikinase', FEBS Letters, vol. 583, no. 7, pp. 1159-1163. https://doi.org/10.1016/j.febslet.2009.02.045

    A CBM20 low-affinity starch-binding domain from glucan, water dikinase. / Christiansen, Camilla; Abou Hachem, Maher; Glaring, M.A.; Vikso-Nielsen, A.; Sigurskjold, B.W.; Svensson, Birte; Blennow, A.

    In: FEBS Letters, Vol. 583, No. 7, 2009, p. 1159-1163.

    Research output: Contribution to journalJournal articleResearchpeer-review

    TY - JOUR

    T1 - A CBM20 low-affinity starch-binding domain from glucan, water dikinase

    AU - Christiansen, Camilla

    AU - Abou Hachem, Maher

    AU - Glaring, M.A.

    AU - Vikso-Nielsen, A.

    AU - Sigurskjold, B.W.

    AU - Svensson, Birte

    AU - Blennow, A.

    PY - 2009

    Y1 - 2009

    N2 - 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.

    AB - 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.

    KW - Carbohydrate-binding module 20

    KW - Starch-binding domain

    KW - Surface plasmon resonance

    KW - Glucan, water dikinase

    KW - Bioimaging

    U2 - 10.1016/j.febslet.2009.02.045

    DO - 10.1016/j.febslet.2009.02.045

    M3 - Journal article

    VL - 583

    SP - 1159

    EP - 1163

    JO - F E B S Letters

    JF - F E B S Letters

    SN - 0014-5793

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    ER -