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Publication Abstract from PubMed

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 beta-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 beta-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 (1.7 A) crystal structure has been determined, resulting in the first reported structure of a GH52 family member. A lower resolution (2.6 A) 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 beta-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.

A novel beta-xylosidase structure from Geobacillus thermoglucosidasius: the first crystal structure of a glycoside hydrolase family GH52 enzyme reveals unpredicted similarity to other glycoside hydrolase folds.,Espina G, Eley K, Pompidor G, Schneider TR, Crennell SJ, Danson MJ Acta Crystallogr D Biol Crystallogr. 2014 May;70(Pt 5):1366-74. doi:, 10.1107/S1399004714002788. Epub 2014 Apr 30. PMID:24816105^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.