A CBM20 low-affinity starch-binding domain from glucan, water dikinase
Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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.
Originalsprog | Engelsk |
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Tidsskrift | FEBS Letters |
Vol/bind | 583 |
Udgave nummer | 7 |
Sider (fra-til) | 1159-1163 |
Antal sider | 5 |
ISSN | 0014-5793 |
DOI | |
Status | Udgivet - 2009 |
ID: 12051736