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. (1st May 2014)

• Record Type: Journal Article
• Authors: Espina, Giannina; Eley, Kirstin; Pompidor, Guillaume; Schneider, Thomas R.; Crennell, Susan J.; Danson, Michael J.
• Is Part Of: Acta crystallographica. Volume 70:Part 5(2014:May)
• Page Start: 1366
• Page End: 1374
• Publication Date: 2014-05-01
• Subjects: Biomolecules -- Structure -- Periodicals; Physical biochemistry -- Periodicals; X-ray crystallography -- Periodicals; Crystallography -- Periodicals; 572
• DOI: 10.1107/S1399004714002788
• Languages: English
• ISSNs: 0907-4449

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <italic>Geobacillus thermoglucosidasius</italic> 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 <italic>G. thermoglucosidasius</italic>β‐xylosidase belonging to CAZy glycoside hydrolase family GH52 has been cloned and expressed in <italic>Escherichia coli</italic>. The recombinant enzyme has been characterized and a high‐resolution (1.7 Å) crystal structure has been determined, resulting in the first reported structure of a GH52 family member. A lower resolution (2.6 Å) 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 <italic>G. thermoglucosidasius</italic>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.</p> </abstract>