Projects per year
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.
|Publication status||Published - 2007|
Subject classification (UKÄ)
- Biochemistry and Molecular Biology
- molecular engineering
- carbohydrate-binding module
- aromatic residue
- binding specificity
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- 1 Finished
Designed carbohydrate binding modules and molecular probes
Ohlin, M., Cicortas Gunnarsson, L., von Schantz, L., Holst, O., Nordberg Karlsson, E. & Logan, D.
2001/01/01 → 2015/12/31