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Crystallization and preliminary crystallographic analysis of exo-alpha-1,5-L-arabinofuranosidase from Streptomyces avermitilis NBRC14893.

ABSTRACT: Exo-alpha-1,5-L-arabinofuranosidase from Streptomyces avermitilis NBRC14893 (SaAraf43A) is composed of a single-chain peptide containing a catalytic domain belonging to glycosyl hydrolase family 43 and a substrate-binding domain belonging to carbohydrate-binding module family 42. The enzyme catalyzes the hydrolysis of an alpha-linked L-arabinofuranosyl residue from hemicelluloses. SaAraf43A was crystallized at 293 K using the sitting-drop vapour-diffusion method. The crystals belonged to space group P2(1)2(1)2(1) and diffracted to a resolution of 2.2 A.

SUBMITTER: Fujimoto Z

PROVIDER: S-EPMC2581701 | biostudies-literature | 2008 Nov

REPOSITORIES: biostudies-literature

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Crystallization and preliminary crystallographic analysis of exo-alpha-1,5-L-arabinofuranosidase from Streptomyces avermitilis NBRC14893.

Fujimoto Zui Z Ichinose Hitomi H Kaneko Satoshi S

Acta crystallographica. Section F, Structural biology and crystallization communications 20081025 Pt 11

Exo-alpha-1,5-L-arabinofuranosidase from Streptomyces avermitilis NBRC14893 (SaAraf43A) is composed of a single-chain peptide containing a catalytic domain belonging to glycosyl hydrolase family 43 and a substrate-binding domain belonging to carbohydrate-binding module family 42. The enzyme catalyzes the hydrolysis of an alpha-linked L-arabinofuranosyl residue from hemicelluloses. SaAraf43A was crystallized at 293 K using the sitting-drop vapour-diffusion method. The crystals belonged to space g ...[more]

PMID: 18997327

Similar Datasets

Characterization of a modular enzyme of exo-1,5-alpha-L-arabinofuranosidase and arabinan binding module from Streptomyces avermitilis NBRC14893.

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