A CBM20 low-affinity starch-binding domain from glucan, water dikinase

Publication: Research - peer-reviewJournal article – Annual report year: 2009

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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.
Original languageEnglish
JournalFEBS Letters
Publication date2009
Volume583
Journal number7
Pages1159-1163
ISSN0014-5793
DOIs
StatePublished
CitationsWeb of Science® Times Cited: 11

Keywords

  • Carbohydrate-binding module 20, Starch-binding domain, Surface plasmon resonance, Glucan, water dikinase, Bioimaging
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