Journal article
A CBM20 low-affinity starch-binding domain from glucan, water dikinase
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.
| Language: | English |
|---|---|
| Year: | 2009 |
| Pages: | 1159-1163 |
| ISSN: | 18733468 and 00145793 |
| Types: | Journal article |
| DOI: | 10.1016/j.febslet.2009.02.045 |
| ORCIDs: | 0000-0002-8003-4635 , 0000-0001-6476-9546 , Abou Hachem, Maher and Svensson, Birte |
Bioimaging Carbohydrate-binding module 20 Glucan, water dikinase Starch-binding domain Surface plasmon resonance
Arabidopsis Arabidopsis Proteins Aspergillus niger Cyclodextrins Cytoplasmic Granules Fungal Proteins Gene Expression Glucan 1,4-alpha-Glucosidase Microscopy, Confocal Nicotiana Phosphotransferases (Paired Acceptors) Protein Binding Protein Structure, Tertiary Starch Structural Homology, Protein alpha-glucan, water dikinase, Arabidopsis
