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A CBM20 low‐affinity starch‐binding domain from glucan, water dikinase
Author(s) -
Christiansen Camilla,
Hachem Maher Abou,
Glaring Mikkel A.,
Viksø-Nielsen Anders,
Sigurskjold Bent W.,
Svensson Birte,
Blennow Andreas
Publication year - 2009
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.02.045
Subject(s) - starch , biochemistry , glucan , chemistry , fluorescence microscope , fluorescence , confocal microscopy , in vitro , fluorescein , carbohydrate binding module , biology , gene , microbiology and biotechnology , physics , quantum mechanics , glycoside hydrolase
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 .