Hexamerní struktura chladově aktivní beta-galaktosidasy z Arthrobacter sp. C2-2

Kód výsledku v IS VaVaI

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Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Hexameric Structure of Cold-Active beta-Galactosidase from Arthrobacter sp. C2-2

Popis výsledku v původním jazyce

Arthrobacter sp. C2-2, a soil bacteria found in Antarctica, belongs to psychrotrophic, i.e. cold tolerant, microorganisms. Two beta-galactosidases, isoenzymes C-2-2-1 and C-2-2-2, were isolated from this bacterium. In this contribution, we would like topresent an X-ray structure of C-2-2-1 beta-galactosidase from Arthrobacter sp. C2-2, which was solved at 1.9 A resolution. The beta-galactosidase belongs to glycosyl hydrolase structural family 2. It is composed of 1023 amino acid residues and can be divided into five structural domains. The active site of the beta-galactosidase is localized within the TIM barrel domain. The beta-galactosidase cleaves beta-galactosides by separating of its terminal galactose group and it also catalyzes transglycosylation. Typically, it cleaves lactose into galactose and glucose. The fold of this beta-galactosidase is similar to that of Escherichia coli, which belongs to the same glycosyl hydrolase family 2 and structure of which was studied in details.

Název v anglickém jazyce

Hexameric Structure of Cold-Active beta-Galactosidase from Arthrobacter sp. C2-2

Popis výsledku anglicky

Arthrobacter sp. C2-2, a soil bacteria found in Antarctica, belongs to psychrotrophic, i.e. cold tolerant, microorganisms. Two beta-galactosidases, isoenzymes C-2-2-1 and C-2-2-2, were isolated from this bacterium. In this contribution, we would like topresent an X-ray structure of C-2-2-1 beta-galactosidase from Arthrobacter sp. C2-2, which was solved at 1.9 A resolution. The beta-galactosidase belongs to glycosyl hydrolase structural family 2. It is composed of 1023 amino acid residues and can be divided into five structural domains. The active site of the beta-galactosidase is localized within the TIM barrel domain. The beta-galactosidase cleaves beta-galactosides by separating of its terminal galactose group and it also catalyzes transglycosylation. Typically, it cleaves lactose into galactose and glucose. The fold of this beta-galactosidase is similar to that of Escherichia coli, which belongs to the same glycosyl hydrolase family 2 and structure of which was studied in details.

Druh

O - Ostatní výsledky

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

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Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2005

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů