| Literature DB >> 19275898 |
Camilla Christiansen1, Maher Abou Hachem, Mikkel A Glaring, Anders Viksø-Nielsen, Bent W Sigurskjold, Birte Svensson, Andreas Blennow.
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.Entities:
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Year: 2009 PMID： 19275898 DOI： 10.1016/j.febslet.2009.02.045
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124