Tine M. Bourgois
Katholieke Universiteit Leuven
Network
Latest external collaboration on country level. Dive into details by clicking on the dots.
Publication
Featured researches published by Tine M. Bourgois.
Biochemical Journal | 2009
Elien Vandermarliere; Tine M. Bourgois; Martyn Winn; Steven Van Campenhout; Guido Volckaert; Jan A. Delcour; Sergei V. Strelkov; Anja Rabijns; Christophe M. Courtin
AXHs (arabinoxylan arabinofuranohydrolases) are alpha-L-arabinofuranosidases that specifically hydrolyse the glycosidic bond between arabinofuranosyl substituents and xylopyranosyl backbone residues of arabinoxylan. Bacillus subtilis was recently shown to produce an AXH that cleaves arabinose units from O-2- or O-3-mono-substituted xylose residues: BsAXH-m2,3 (B. subtilis AXH-m2,3). Crystallographic analysis reveals a two-domain structure for this enzyme: a catalytic domain displaying a five-bladed beta-propeller fold characteristic of GH (glycoside hydrolase) family 43 and a CBM (carbohydrate-binding module) with a beta-sandwich fold belonging to CBM family 6. Binding of substrate to BsAXH-m2,3 is largely based on hydrophobic stacking interactions, which probably allow the positional flexibility needed to hydrolyse both arabinose substituents at the O-2 or O-3 position of the xylose unit. Superposition of the BsAXH-m2,3 structure with known structures of the GH family 43 exo-acting enzymes, beta-xylosidase and alpha-L-arabinanase, each in complex with their substrate, reveals a different orientation of the sugar backbone.
Biochemical Journal | 2008
Elien Vandermarliere; Tine M. Bourgois; Sigrid Rombouts; Steven Van Campenhout; Guido Volckaert; Sergei V. Strelkov; Jan A. Delcour; Anja Rabijns; Christophe M. Courtin
GH 11 (glycoside hydrolase family 11) xylanases are predominant enzymes in the hydrolysis of heteroxylan, an abundant structural polysaccharide in the plant cell wall. To gain more insight into the protein-ligand interactions of the glycone as well as the aglycone subsites of these enzymes, catalytically incompetent mutants of the Bacillus subtilis and Aspergillus niger xylanases were crystallized, soaked with xylo-oligosaccharides and subjected to X-ray analysis. For both xylanases, there was clear density for xylose residues in the -1 and -2 subsites. In addition, for the B. subtilis xylanase, there was also density for xylose residues in the -3 and +1 subsite showing the spanning of the -1/+1 subsites. These results, together with the observation that some residues in the aglycone subsites clearly adopt a different conformation upon substrate binding, allowed us to identify the residues important for substrate binding in the aglycone subsites. In addition to substrate binding in the active site of the enzymes, the existence of an unproductive second ligand-binding site located on the surface of both the B. subtilis and A. niger xylanases was observed. This extra binding site may have a function similar to the separate carbohydrate-binding modules of other glycoside hydrolase families.
Applied and Environmental Microbiology | 2007
Stijn Lagaert; Steven Van Campenhout; Annick Pollet; Tine M. Bourgois; Jan A. Delcour; Christophe M. Courtin; Guido Volckaert
ABSTRACT The family 8 glycoside hydrolase (RexA) from Bifidobacterium adolescentis was expressed in Escherichia coli. The recombinant enzyme was characterized as a reducing-end xylose-releasing exo-oligoxylanase. Apart from giving insights into this new class of enzymes, knowledge of the RexA enzyme helps to postulate a mechanism for the B. adolescentis breakdown of prebiotic xylooligosaccharides.
Acta Crystallographica Section F-structural Biology and Crystallization Communications | 2007
Elien Vandermarliere; Tine M. Bourgois; Steven Van Campenhout; Sergei V. Strelkov; Guido Volckaert; Jan A. Delcour; Christophe M. Courtin; Anja Rabijns
Arabinoxylan arabinofuranohydrolases (AXH) are alpha-L-arabinofuranosidases (EC 3.2.1.55) that specifically hydrolyse the glycosidic bond between arabinofuranosyl substituents and xylopyranosyl residues from arabinoxylan, hence their name. In this study, the crystallization and preliminary X-ray analysis of the AXH from Bacillus subtilis, a glycoside hydrolase belonging to family 43, is described. Purified recombinant AXH crystallized in the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 68.7, b = 73.7, c = 106.5 A. X-ray diffraction data were collected to a resolution of 1.55 A.
Applied Microbiology and Biotechnology | 2007
Tine M. Bourgois; Valerie Van Craeyveld; Steven Van Campenhout; Christophe M. Courtin; Jan A. Delcour; Johan Robben; Guido Volckaert
Biochemical and Biophysical Research Communications | 2007
Steven Van Campenhout; Annick Pollet; Tine M. Bourgois; Sigrid Rombouts; Johnny Beaugrand; Kurt Gebruers; Evelien De Backer; Christophe M. Courtin; Jan A. Delcour; Guido Volckaert
Journal of Biotechnology | 2007
Tine M. Bourgois; Dung V. Nguyen; Stefaan Sansen; Sigrid Rombouts; Tim Beliën; Katleen Fierens; Gert Raedschelders; Anja Rabijns; Christophe M. Courtin; Jan A. Delcour; Steven Van Campenhout; Guido Volckaert
Journal of Molecular Recognition | 2007
Tim Beliën; Steven Van Campenhout; An Vanden Bosch; Tine M. Bourgois; Sigrid Rombouts; Johan Robben; Christophe M. Courtin; Jan A. Delcour; Guido Volckaert
Enzyme and Microbial Technology | 2007
Karolien Moers; Tine M. Bourgois; Sigrid Rombouts; Tim Beliën; Steven Van Campenhout; Guido Volckaert; Johan Robben; Kristof Brijs; Jan A. Delcour; Christophe M. Courtin
Archive | 2006
Tine M. Bourgois; Steven Van Campenhout; Valerie Van Craeyveld; Christophe Courtin; Jan Delcour; Guido Volckaert