A CBM20 low-affinity starch-binding domain from glucan, water dikinase
- Christiansen, Camilla
- Hachem, Maher Abou
- Glaring, Mikkel A.
- Viksø-Nielsen, Anders
- Sigurskjold, Bent W.
- Svensson, Birte
- Blennow, Andreas
Publication date
April 2009
DOI Publisher
Federation of European Biochemical Societies. Published by Elsevier B.V.Abstract
AbstractThe 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
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