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Novel xylan-binding properties of an engineered family 4 carbohydrate-binding module

Cicortas Gunnarsson, Lavinia LU ; Montanier, Cedric; Tunnicliffe, Richard B.; Williamson, Mike R.; Gilbert, Harry J.; Nordberg Karlsson, Eva LU and Ohlin, Mats LU (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)
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author
organization
publishing date
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 Limited
external identifiers
  • wos:000249181200003
  • scopus:34548178992
ISSN
0264-6021
DOI
10.1042/BJ20070128
language
English
LU publication?
yes
id
a3e7378d-88ce-480e-a555-8263d68f47fc (old id 689640)
date added to LUP
2007-12-07 13:50:47
date last changed
2017-09-03 04:39:08
@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},
  keyword      = {thermodynamics,molecular engineering,carbohydrate-binding module,aromatic residue,binding specificity,xylan},
  language     = {eng},
  pages        = {209--214},
  publisher    = {Portland Press Limited},
  series       = {Biochemical Journal},
  title        = {Novel xylan-binding properties of an engineered family 4 carbohydrate-binding module},
  url          = {http://dx.doi.org/10.1042/BJ20070128},
  volume       = {406},
  year         = {2007},
}