A novel β-xylosidase structure from Geobacillus thermoglucosidasius: The first crystal structure of a glycoside hydrolase family GH52 enzyme reveals unpredicted similarity to other glycoside hydrolase folds

Giannina Espina Silva, Kirstin Eley, Guillaume Pompidor, Thomas R. Schneider, Susan J. Crennell, Michael J. Danson

Research output: Contribution to journalArticle

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Abstract

Geobacillus thermoglucosidasius is a thermophilic bacterium that is able to ferment both C6 and C5 sugars to produce ethanol. During growth on hemicellulose biomass, an intracellular β-xylosidase catalyses the hydrolysis of xylo-oligosaccharides to the monosaccharide xylose, which can then enter the pathways of central metabolism. The gene encoding a G. thermoglucosidasius β-xylosidase belonging to CAZy glycoside hydrolase family GH52 has been cloned and expressed in Escherichia coli. The recombinant enzyme has been characterized and a high-resolution (1.7Å) crystal structure has been determined, resulting in the first reported structure of a GH52 family member. A lower resolution (2.6Å) structure of the enzyme-substrate complex shows the positioning of the xylobiose substrate to be consistent with the proposed retaining mechanism of the family; additionally, the deep cleft of the active-site pocket, plus the proximity of the neighbouring subunit, afford an explanation for the lack of catalytic activity towards the polymer xylan. Whilst the fold of the G. thermoglucosidasius β-xylosidase is completely different from xylosidases in other CAZy families, the enzyme surprisingly shares structural similarities with other glycoside hydrolases, despite having no more than 13% sequence identity.
Original languageEnglish
Pages (from-to)1366-1374
Number of pages9
JournalActa Crystallographica Section D-Biological Crystallography
Volume70
Issue number5
DOIs
Publication statusPublished - 1 May 2014

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