4C1O

Geobacillus thermoglucosidasius GH family 52 xylosidase

4C1O の概要

• エントリーDOI: 10.2210/pdb4c1o/pdb
• 関連するPDBエントリー: 4C1P
• 分子名称: BETA-XYLOSIDASE, SULFATE ION, SODIUM ION, ... (8 entities in total)
• 機能のキーワード: hydrolase, gh52
• 由来する生物種: Geobacillus thermoglucosidasius
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 85163.66

構造登録者

Espina, G.,Eley, K.,Schneider, T.R.,Crennell, S.J.,Danson, M.J. (登録日: 2013-08-13, 公開日: 2014-05-14, 最終更新日: 2024-05-08)

主引用文献

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

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: 24816105
DOI: 10.1107/S1399004714002788

実験手法

X-RAY DIFFRACTION (1.7 Å)