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Wiley, FEBS Letters, 7(583), p. 1159-1163, 2009

DOI: 10.1016/j.febslet.2009.02.045

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A CBM20 low-affinity starch binding domain from Glucan, Water Dikinase

Journal article published in 2009 by Camilla Christiansen, Maher Abou Hachem ORCID, Mikkel A. Glaring, Anders Viksø-Nielsen, Bent W. Sigurskjold, Birte Svensson, Andreas Blennow
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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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.