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

Camilla Christiansen; Maher Abou Hachem; Mikkel Andreas Glaring; Anders Viksø-Nielsen; Bent Walther Sigurskjold; Birte Svensson; Per Gunnar Andreas Blennow

doi:10.1016/j.febslet.2009.02.045

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

Camilla Christiansen, Maher Abou Hachem, Mikkel Andreas Glaring, Anders Viksø-Nielsen, Bent Walther Sigurskjold, Birte Svensson, Per Gunnar Andreas Blennow

Biomolecular Sciences

33 Citations (Scopus)

Abstract

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 language	English
Journal	FEBS Letters
Volume	583
Issue number	7
Pages (from-to)	1159-1163
Number of pages	5
ISSN	0014-5793
DOIs	https://doi.org/10.1016/j.febslet.2009.02.045
Publication status	Published - 2009

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10.1016/j.febslet.2009.02.045

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@article{980cf590332b11de87b8000ea68e967b,

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

abstract = "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.",

author = "Camilla Christiansen and {Abou Hachem}, Maher and Glaring, {Mikkel Andreas} and Anders Viks{\o}-Nielsen and Sigurskjold, {Bent Walther} and Birte Svensson and Blennow, {Per Gunnar Andreas}",

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

year = "2009",

doi = "10.1016/j.febslet.2009.02.045",

language = "English",

volume = "583",

pages = "1159--1163",

journal = "F E B S Letters",

issn = "0014-5793",

publisher = "JohnWiley & Sons Ltd",

number = "7",

}

TY - JOUR

T1 - A CBM20 low-affinity starch-binding domain from glucan, water dikinase

AU - Christiansen, Camilla

AU - Abou Hachem, Maher

AU - Glaring, Mikkel Andreas

AU - Viksø-Nielsen, Anders

AU - Sigurskjold, Bent Walther

AU - Svensson, Birte

AU - Blennow, Per Gunnar Andreas

N1 - Keywords: Bioimaging; Carbohydrate-binding module 20; Glucan, water dikinase; Starch-binding domain; Surface plasmon resonance

PY - 2009

Y1 - 2009

N2 - 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.

AB - 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.

U2 - 10.1016/j.febslet.2009.02.045

DO - 10.1016/j.febslet.2009.02.045

M3 - Journal article

C2 - 19275898

SN - 0014-5793

VL - 583

SP - 1159

EP - 1163

JO - F E B S Letters

JF - F E B S Letters

IS - 7

ER -

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

Abstract

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