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The crystal structure of XG-34, an evolved xyloglucan-specific carbohydrate-binding module
KTH, School of Biotechnology (BIO), Glycoscience.
KTH, School of Biotechnology (BIO), Glycoscience.
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2010 (English)In: Proteins: Structure, Function, and Genetics, ISSN 0887-3585, E-ISSN 1097-0134, Vol. 78, no 3, 785-789 p.Article in journal (Refereed) Published
Place, publisher, year, edition, pages
2010. Vol. 78, no 3, 785-789 p.
Keyword [en]
CBM, carbohydrate-binding module, crystal structure, thermostable, non-fucosylated xyloglucan, Rhodothermus marinus, rhodothermus-marinus, trichoderma-reesei, catalytic core, recognition, xylanase, refinement, diversity, cbm4-2, models, domain
National Category
Biochemistry and Molecular Biology Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:kth:diva-19143DOI: 10.1002/prot.22642ISI: 000273923700025OAI: oai:DiVA.org:kth-19143DiVA: diva2:337190
Funder
FormasSwedish Research Council
Note
QC 20100902Available from: 2010-08-05 Created: 2010-08-05 Last updated: 2017-12-12Bibliographically approved
In thesis
1. On the engineering of proteins: methods and applications for carbohydrate-active enzymes
Open this publication in new window or tab >>On the engineering of proteins: methods and applications for carbohydrate-active enzymes
2010 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

This thesis presents the application of different protein engineering methods on enzymes and non-catalytic proteins that act upon xyloglucans. Xyloglucans are polysaccharides found as storage polymers in seeds and tubers, and as cross-linking glucans in the cell wall of plants. Their structure is complex with intricate branching patterns, which contribute to the physical properties of the polysaccharide including its binding to and interaction with other glucans such as cellulose.

One important group of xyloglucan-active enzymes is encoded by the GH16 XTH gene family in plants, including xyloglucan endo-transglycosylases (XET) and xyloglucan endo-hydrolases (XEH). The molecular determinants behind the different catalytic routes of these homologous enzymes are still not fully understood. By combining structural data and molecular dynamics (MD) simulations, interesting facts were revealed about enzyme-substrate interaction. Furthermore, a pilot study was performed using structure-guided recombination to generate a restricted library of XET/XEH chimeras.

Glycosynthases are hydrolytically inactive mutant glycoside hydrolases (GH) that catalyse the formation of glycosidic linkages between glycosyl fluoride donors and glycoside acceptors. Different enzymes with xyloglucan hydrolase activity were engineered into glycosynthases, and characterised as tools for the synthesis of well-defined homogenous xyloglucan oligo- and polysaccharides with regular substitution patterns.

Carbohydrate-binding modules (CBM) are non-catalytic protein domains that bind to polysaccharidic substrates. An important technical application involves their use as molecular probes to detect and localise specific carbohydrates in vivo. The three-dimensional structure of an evolved xyloglucan binding module (XGBM) was solved by X-ray diffraction. Affinity-guided directed evolution of this first generation XGBM resulted in highly specific probes that were used to localise non-fucosylated xyloglucans in plant tissue sections.

Place, publisher, year, edition, pages
Stockholm: KTH, 2010. xii, 74 p.
Series
Trita-BIO-Report, ISSN 1654-2312 ; 2010:14
Keyword
enzyme engineering, rational design, directed evolution, DNA shuffling, glycosynthase, xyloglucan, xyloglucan endo-transglycosylase, retaining glycoside hydrolase, xyloglucanase, carbohydrate binding module, polysaccharide synthesis
National Category
Industrial Biotechnology
Identifiers
urn:nbn:se:kth:diva-24296 (URN)978-91-7415-709-3 (ISBN)
Public defence
2010-09-22, FD5, AlbaNova Universitetscentrum, Roslagstullsbacken 21, Stockholm, 10:15 (English)
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Note
QC 20100902Available from: 2010-09-02 Created: 2010-08-31 Last updated: 2010-09-02Bibliographically approved

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Divne, Christina

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