Publications by authors named "E V Eneiskaya"
The enzyme beta-xylosidase from Trichoderma reesei, a member of glycosil hydrolase family 3 (GH3), is a glycoside hydrolase which acts at the glycosidic linkages of 1,4-beta-xylooligosaccharides and that also exhibits alpha-l-arabinofuranosidase activity on 4-nitrophenyl alpha-l-arabinofuranoside. In this work, we show that the enzyme forms monomers in solution and derive the low-resolution molecular envelope of the beta-xylosidase from small-angle X-ray scattering (SAXS) data using the ab initio simulated annealing algorithm. The radius of gyration and the maximum dimension of the beta-xylosidase are 30.
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- A molecular envelope of beta-mannosidase from Trichoderma reesei was created using small-angle X-ray scattering (SAXS) and crystallography, revealing its protein shape.
- Crystallographic data improved the SAXS findings, and similarity between beta-mannosidase and beta-galactosidase was noted, demonstrating comparable three-dimensional structures.
- The combined techniques of distance distribution functions, 1D and 2D sequence alignment successfully narrowed down structurally similar proteins and may be useful in broader structural genomics research.
Crystallization and preliminary X-ray study of beta--mannosidase from Trichoderma reesei.
Acta Crystallogr D Biol Crystallogr
March 2000
beta-Mannosidase from Trichoderma reesei, a 105 kDa glycoprotein, has been crystallized. The crystals belong to the space group P4(1)2(1)2 or P4(3)2(1)2, with unit-cell dimensions a = b = 165.86, c = 122.
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