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Crystallization and preliminary crystallographic analysis of the glycoside hydrolase family 115 ?-glucuronidase from Streptomyces pristinaespiralis.

ABSTRACT: ?-Glucuronidase from Streptomyces pristinaespiralis (SpGlcA115A) is composed of a single-chain peptide containing a catalytic domain belonging to glycosyl hydrolase family 115, a novel family of hemicellulolytic ?-glucuronidases. The enzyme catalyzes the hydrolysis of ?-linked 4-O-methylglucuronosyl and glucuronosyl residues from both polymeric xylans and oligosaccharides. SpGlcA115A was crystallized at 293?K using the sitting-drop vapour-diffusion method. The crystals belonged to space group R3 and diffracted to a resolution of 1.9?Å.

SUBMITTER: Fujimoto Z

PROVIDER: S-EPMC3079975 | biostudies-literature | 2011 Jan

REPOSITORIES: biostudies-literature

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Crystallization and preliminary crystallographic analysis of the glycoside hydrolase family 115 α-glucuronidase from Streptomyces pristinaespiralis.

Fujimoto Zui Z Ichinose Hitomi H Biely Peter P Kaneko Satoshi S

Acta crystallographica. Section F, Structural biology and crystallization communications 20101222 Pt 1

α-Glucuronidase from Streptomyces pristinaespiralis (SpGlcA115A) is composed of a single-chain peptide containing a catalytic domain belonging to glycosyl hydrolase family 115, a novel family of hemicellulolytic α-glucuronidases. The enzyme catalyzes the hydrolysis of α-linked 4-O-methylglucuronosyl and glucuronosyl residues from both polymeric xylans and oligosaccharides. SpGlcA115A was crystallized at 293 K using the sitting-drop vapour-diffusion method. The crystals belonged to space group R3 ...[more]

PMID: 21206027

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