Novel xylan-binding properties of an engineered family 4 carbohydrate-binding module
(2007) In Biochemical Journal 406. p.209-214- 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... (More)
- 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. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/689640
- author
- Cicortas Gunnarsson, Lavinia LU ; Montanier, Cedric ; Tunnicliffe, Richard B. ; Williamson, Mike R. ; Gilbert, Harry J. ; Nordberg Karlsson, Eva LU and Ohlin, Mats LU
- organization
- publishing date
- 2007
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- thermodynamics, molecular engineering, carbohydrate-binding module, aromatic residue, binding specificity, xylan
- in
- Biochemical Journal
- volume
- 406
- pages
- 209 - 214
- publisher
- Portland Press
- external identifiers
-
- wos:000249181200003
- scopus:34548178992
- ISSN
- 0264-6021
- DOI
- 10.1042/BJ20070128
- project
- Designed carbohydrate binding modules and molecular probes
- language
- English
- LU publication?
- yes
- id
- a3e7378d-88ce-480e-a555-8263d68f47fc (old id 689640)
- date added to LUP
- 2016-04-01 16:39:35
- date last changed
- 2022-01-28 21:12:18
@article{a3e7378d-88ce-480e-a555-8263d68f47fc, 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.}}, author = {{Cicortas Gunnarsson, Lavinia and Montanier, Cedric and Tunnicliffe, Richard B. and Williamson, Mike R. and Gilbert, Harry J. and Nordberg Karlsson, Eva and Ohlin, Mats}}, issn = {{0264-6021}}, keywords = {{thermodynamics; molecular engineering; carbohydrate-binding module; aromatic residue; binding specificity; xylan}}, language = {{eng}}, pages = {{209--214}}, publisher = {{Portland Press}}, series = {{Biochemical Journal}}, title = {{Novel xylan-binding properties of an engineered family 4 carbohydrate-binding module}}, url = {{http://dx.doi.org/10.1042/BJ20070128}}, doi = {{10.1042/BJ20070128}}, volume = {{406}}, year = {{2007}}, }