4C1P
Geobacillus thermoglucosidasius GH family 52 xylosidase
Summary for 4C1P
| Entry DOI | 10.2210/pdb4c1p/pdb |
| Related | 4C1O |
| Related PRD ID | PRD_900116 |
| Descriptor | BETA-XYLOSIDASE, beta-D-xylopyranose-(1-4)-beta-D-xylopyranose, SODIUM ION, ... (5 entities in total) |
| Functional Keywords | hydrolase, gh52, xylobiose |
| Biological source | GEOBACILLUS THERMOGLUCOSIDASIUS |
| Total number of polymer chains | 1 |
| Total formula weight | 82611.06 |
| Authors | Espina, G.,Eley, K.,Schneider, T.R.,Crennell, S.J.,Danson, M.J. (deposition date: 2013-08-13, release date: 2014-05-14, Last modification date: 2024-05-01) |
| Primary citation | Espina, G.,Eley, K.,Pompidor, G.,Schneider, T.R.,Crennell, S.J.,Danson, M.J. 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 Acta Crystallogr.,Sect.D, 70:1366-, 2014 Cited by PubMed 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 (1.7 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 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. PubMed: 24816105DOI: 10.1107/S1399004714002788 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.634 Å) |
Structure validation
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