Crystallization and preliminary crystallographic analysis of a thermostable family 52 beta-D-xylosidase from Geobacillus stearothermophilus T-6.
نویسندگان
چکیده
Beta-D-xylosidases (EC 3.2.1.37) are hemicellulases that hydrolyze short xylooligosaccharides into single xylose units. In this study, the first crystallization and preliminary X-ray analysis of a family 52 glycoside hydrolase, the beta-D-xylosidase (XynB2) from Geobacillus stearothermophilus T-6, is described. XynB2 is a dimeric protein consisting of two identical subunits of 705 amino acids with a calculated molecular weight of 79 894 Da. XynB2 was crystallized by the hanging-drop vapour-diffusion method and the crystals were found to belong to space group P1, with unit-cell parameters a = 80.6, b = 97.5, c = 107.2 A, alpha = 107.4, beta = 98.2, gamma = 106.6 degrees. The native crystals diffracted X-rays to a resolution of 2.0 A.
منابع مشابه
Enzyme-substrate complex structures of a GH39 beta-xylosidase from Geobacillus stearothermophilus.
Beta-D-Xylosidases are glycoside hydrolases that catalyse the release of xylose units from short xylooligosaccharides and are engaged in the final breakdown of plant cell-wall hemicelluloses. beta-D-Xylosidases are found in glycoside hydrolase families 3, 39, 43, 52 and 54. The first crystal structure of a GH39 beta-xylosidase revealed a multi-domain organization with the catalytic domain havin...
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beta-D-Xylosidases are glycoside hydrolases that catalyze the release of xylose units from short xylooligosaccharides and are engaged in the final breakdown of plant cell-wall hemicellulose. Here we describe the enzyme-substrate crystal structure of an inverting family 43 beta-xylosidase, from Geobacillus stearothermophilus T-6 (XynB3). Each XynB3 monomeric subunit is organized in two domains: ...
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ورودعنوان ژورنال:
- Acta crystallographica. Section D, Biological crystallography
دوره 60 Pt 8 شماره
صفحات -
تاریخ انتشار 2004