Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 448581
Title Crystal structure of endo-xylogalacturonan hydrolase from Aspergillus tubingensis
Author(s) Rozeboom, H.J.; Beldman, G.; Schols, H.A.; Dijkstra, B.W.
Source FEBS Journal 280 (2013)23. - ISSN 1742-464X - p. 6061 - 6069.
DOI https://doi.org/10.1111/febs.12524
Department(s) Food Chemistry
VLAG
Publication type Refereed Article in a scientific journal
Publication year 2013
Keyword(s) site-directed mutagenesis - endopolygalacturonase ii - sequence alignments - features - polysaccharides - processivity - degradation - pectin - niger - polygalacturonase
Abstract Endo-xylogalacturonan hydrolase is a member of glycoside hydrolase family 28 (GH28) that hydrolyzes the glycosidic bond between two ß-xylose-substituted galacturonic acid residues in pectin. Presented here is the X-ray crystal structure of the endo-xylogalacturonan hydrolase from Aspergillus tubingensis (XghA) at 1.75 Å resolution. The high degree of structural conservation in the active site and catalytic apparatus compared with polygalacturonases indicates that cleavage of the substrate proceeds in essentially the same way as found for the other GH28 enzymes. Molecular modeling of a xylosylated tri-galacturonate in the active site identified the amino acid residues involved in substrate binding. They border a substrate-binding cleft that is much wider than in other polygalacturonases, and can accommodate xylosylated substrates. The most extensive interactions appear to occur at subsite +2, in agreement with the enzyme kinetics results, which showed enhanced activity on substrates with a xylose attached to the galacturonic acid bound at subsite +2
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