期刊
FEBS LETTERS
卷 583, 期 7, 页码 1159-1163出版社
WILEY
DOI: 10.1016/j.febslet.2009.02.045
关键词
Bioimaging; Carbohydrate-binding module 20; Glucan, water dikinase; Starch-binding domain; Surface plasmon resonance
资金
- Danish Natural Science Research Council
- Danish Research Council for Technology and Production Sciences
- Carlsberg Foundation
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. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据