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Abstract
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, CBM42 from the Rhodothermits marinus xylanase Xyn10A, and the identification of the X-2 variant. As compared with the wildtype 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.
Original language | English |
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Pages (from-to) | 209-214 |
Journal | Biochemical Journal |
Volume | 406 |
DOIs | |
Publication status | Published - 2007 |
Subject classification (UKÄ)
- Biological Sciences
Free keywords
- thermodynamics
- molecular engineering
- carbohydrate-binding module
- aromatic residue
- binding specificity
- xylan
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Dive into the research topics of 'Novel xylan-binding properties of an engineered family 4 carbohydrate-binding module'. Together they form a unique fingerprint.Projects
- 1 Finished
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Designed carbohydrate binding modules and molecular probes
Ohlin, M. (PI), Cicortas Gunnarsson, L. (Research student), von Schantz, L. (Research student), Holst, O. (Assistant supervisor), Nordberg Karlsson, E. (Assistant supervisor) & Logan, D. (Researcher)
2001/01/01 → 2015/12/31
Project: Research