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Crystallization and preliminary crystallographic analysis of the family GH78 alpha-L-rhamnosidase RhaB from Bacillus sp. GL1.

ABSTRACT: Alpha-L-rhamnosidases play important roles in the metabolism of plant cell walls, glycosides and bacterial biofilms. This enzyme is also used industrially for debittering citrus fruits by releasing rhamnose from the plant flavonoid naringin. Bacillus sp. GL1 alpha-L-rhamnosidase (RhaB) is a member of glycoside hydrolase (GH) family 78. Native and selenomethionine-derivative enzymes were crystallized at 293 K by hanging-drop vapour diffusion with polyethylene glycol 8000 as a precipitant. This is the first report of the crystallization of a family GH78 enzyme.

SUBMITTER: Cui Z

PROVIDER: S-EPMC2242939 | biostudies-literature | 2006 Jul

REPOSITORIES: biostudies-literature

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Crystallization and preliminary crystallographic analysis of the family GH78 alpha-L-rhamnosidase RhaB from Bacillus sp. GL1.

Cui Zhongli Z Maruyama Yukie Y Mikami Bunzo B Hashimoto Wataru W Murata Kousaku K

Acta crystallographica. Section F, Structural biology and crystallization communications 20060610 Pt 7

Alpha-L-rhamnosidases play important roles in the metabolism of plant cell walls, glycosides and bacterial biofilms. This enzyme is also used industrially for debittering citrus fruits by releasing rhamnose from the plant flavonoid naringin. Bacillus sp. GL1 alpha-L-rhamnosidase (RhaB) is a member of glycoside hydrolase (GH) family 78. Native and selenomethionine-derivative enzymes were crystallized at 293 K by hanging-drop vapour diffusion with polyethylene glycol 8000 as a precipitant. This is ...[more]

PMID: 16820683

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