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Novel xylan-binding...
Novel xylan-binding properties of an engineered family 4 carbohydrate-binding module
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- Cicortas Gunnarsson, Lavinia (författare)
- Lund University,Lunds universitet,Institutionen för immunteknologi,Institutioner vid LTH,Lunds Tekniska Högskola,Department of Immunotechnology,Departments at LTH,Faculty of Engineering, LTH,Department of Immunotechnology, Lund University, Lund, Sweden
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- Montanier, Cedric (författare)
- Institute for Cell and Molecular Biosciences, University of Newcastle upon Tyne, Newcastle upon Tyne, UK
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- Tunnicliffe, Richard B. (författare)
- Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, UK
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Williamson, Mike R. (författare)
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- Gilbert, Harry J. (författare)
- Institute for Cell and Molecular Biosciences, University of Newcastle upon Tyne, Newcastle upon Tyne, UK
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- Nordberg Karlsson, Eva (författare)
- Lund University,Lunds universitet,Bioteknik,Centrum för tillämpade biovetenskaper,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biotechnology,Center for Applied Life Sciences,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH,Department of Biotechnology, Lund University, Lund, Sweden
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- Ohlin, Mats (författare)
- Lund University,Lunds universitet,Institutionen för immunteknologi,Institutioner vid LTH,Lunds Tekniska Högskola,Department of Immunotechnology,Departments at LTH,Faculty of Engineering, LTH,Department of Immunotechnology, Lund University, Lund, Sweden
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- Williamson, Mike P (författare)
- Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, UK
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(creator_code:org_t)
- Portland Press, 2007
- 2007
- Engelska.
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Ingår i: Biochemical Journal. - : Portland Press. - 0264-6021 .- 1470-8728. ; 406, s. 209-214
- Relaterad länk:
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http://dx.doi.org/10...
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https://lup.lub.lu.s...
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https://doi.org/10.1...
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https://urn.kb.se/re...
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Abstract
Ämnesord
Stäng
- 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.
Ämnesord
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Nyckelord
- thermodynamics
- molecular engineering
- carbohydrate-binding module
- aromatic residue
- binding specificity
- xylan
- aromatic residue; binding specificity; carbohydrate-binding module; molecular engineering; thermodynamics; xylan
Publikations- och innehållstyp
- art (ämneskategori)
- ref (ämneskategori)
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