Novel xylan-binding properties of an engineered family 4 carbohydrate-binding module
Författare
Summary, in English
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.
Avdelning/ar
Publiceringsår
2007
Språk
Engelska
Sidor
209-214
Publikation/Tidskrift/Serie
Biochemical Journal
Volym
406
Dokumenttyp
Artikel i tidskrift
Förlag
Portland Press
Ämne
- Biochemistry and Molecular Biology
Nyckelord
- thermodynamics
- molecular engineering
- carbohydrate-binding module
- aromatic residue
- binding specificity
- xylan
Status
Published
Projekt
- Designed carbohydrate binding modules and molecular probes
ISBN/ISSN/Övrigt
- ISSN: 0264-6021