NDLI: Critical roles of Asp270 and Trp273 in the α-repeat of the carbohydrate-binding module of endo-1,3-β-glucanase for laminarin-binding avidity

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Critical roles of Asp270 and Trp273 in the α-repeat of the carbohydrate-binding module of endo-1,3-β-glucanase for laminarin-binding avidity

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Critical roles of Asp270 and Trp273 in the α-repeat of the carbohydrate-binding module of endo-1,3-β-glucanase for laminarin-binding avidity

Content Provider	Springer Nature Link
Author	Tamashiro, Tomonari Tanabe, Yoichi Ikura, Teikichi Ito, butoshi Oda, Masayuki
Copyright Year	2011
Abstract	A carbohydrate-binding module from family 13 (CBM13), appended to the catalytic domain of endo-1,3-β-glucanase from Cellulosimicrobium cellulans, was overexpressed in E. coli, and its interactions with β-glucans, laminarin and laminarioligosaccharides, were analyzed using surface plasmon resonance biosensor and isothermal titration calorimetry. The association constants for laminarin and laminarioligosaccharides were determined to be approximately 106 M−1 and 104 M−1, respectively, indicating that 2 or 3 binding sites in the α-, β-, and γ-repeats of CBM13 are involved in laminarin binding in a cooperative manner. The binding avidity is approximately 2-orders higher than the monovalent binding affinity. Mutational analysis of the conserved Asp residues in the respective repeats showed that the α-repeat primarily contributes to β-glucan binding. A Trp residue is predicted to be exposed to the solvent only in the α-repeat and would contribute to β-glucan binding. The α-repeat bound β-glucan with an affinity of approximately 104 M−1, and the other repeats additionally bound laminarin, resulting in the increased binding avidity. This binding is unique compared to the recognition mode of another CBM13 from Streptomyces lividans xylanase.
Starting Page	77
Ending Page	85
Page Count	9
File Format	PDF
ISSN	02820080
Journal	Glycoconjugate Journal
Volume Number	29
Issue Number	1
e-ISSN	15734986
Language	English
Publisher	Springer US
Publisher Date	2011-12-27
Publisher Place	Boston
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Carbohydrate-binding module β-glucan Affinity and avidity Site-directed mutagenesis Biomolecular interaction Biochemistry Pathology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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