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

Research output: Contribution to journal › Journal article › Research › peer-review

  • Camilla Christiansen
  • Maher Abou Hachem
  • Mikkel Andreas Glaring
  • Anders Viksø-Nielsen
  • Bent Walther Sigurskjold
  • Birte Svensson
  • Blennow, Andreas
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
Volume583
Issue number7
Pages (from-to)1159-1163
Number of pages5
ISSN0014-5793
DOIs
Publication statusPublished - 2009

Bibliographical note

Keywords: Bioimaging; Carbohydrate-binding module 20; Glucan, water dikinase; Starch-binding domain; Surface plasmon resonance

ID: 12051736