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Novel xylan-binding properties of an engineered family 4 carbohydrate-binding module
Department of Immunotechnology, Lund University, Lund, Sweden.
Institute for Cell and Molecular Biosciences, University of Newcastle upon Tyne, Newcastle upon Tyne, UK.
Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, UK.
Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, UK.
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2007 (English)In: Biochemical Journal, ISSN 0264-6021, E-ISSN 1470-8728, Vol. 406, no 2, p. 209-214Article in journal (Refereed) Published
Abstract [en]

Molecular engineering of ligand-binding proteins is commonly used for identification of variants that display novel specificities. Using this approach to introduce novel specificities into CBMs (carbohydrate-binding modules) has not been extensively explored. Here, we report the engineering of a CBM, CBM4-2 from the Rhodothermus marinus xylanase Xyn10A, and the identification of the X-2 variant. As compared with the wild-type protein, this engineered module displays higher specificity for the polysaccharide xylan, and a lower preference for binding xylo-oligomers rather than binding the natural decorated polysaccharide. The mode of binding of X-2 differs from other xylan-specific CBMs in that it only has one aromatic residue in the binding site that can make hydrophobic interactions with the sugar rings of the ligand. The evolution of CBM4-2 has thus generated a xylan-binding module with different binding properties to those displayed by CBMs available in Nature.

Place, publisher, year, edition, pages
Portland Press, 2007. Vol. 406, no 2, p. 209-214
Keywords [en]
aromatic residue; binding specificity; carbohydrate-binding module; molecular engineering; thermodynamics; xylan
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:oru:diva-64488DOI: 10.1042/BJ20070128ISI: 000249181200003PubMedID: 17506724Scopus ID: 2-s2.0-34548178992OAI: oai:DiVA.org:oru-64488DiVA, id: diva2:1177100
Note

Funding Agency:

Biotechnology and Biological Sciences Research Council  BB/C005074/1

Available from: 2018-01-24 Created: 2018-01-24 Last updated: 2018-01-26Bibliographically approved

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Gunnarsson, Lavinia Cicortas

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