About: Hexameric Structure of Cold-Active beta-Galactosidase from Arthrobacter sp. C2-2     Goto   Sponge   NotDistinct   Permalink

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  • 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 to present 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. It is known that
  • 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 to present 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. It is known that (en)
  • 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 to present 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. It is known that (cs)
Title
  • Hexameric Structure of Cold-Active beta-Galactosidase from Arthrobacter sp. C2-2
  • Hexameric Structure of Cold-Active beta-Galactosidase from Arthrobacter sp. C2-2 (en)
  • Hexamerní struktura chladově aktivní beta-galaktosidasy z Arthrobacter sp. C2-2 (cs)
skos:prefLabel
  • Hexameric Structure of Cold-Active beta-Galactosidase from Arthrobacter sp. C2-2
  • Hexameric Structure of Cold-Active beta-Galactosidase from Arthrobacter sp. C2-2 (en)
  • Hexamerní struktura chladově aktivní beta-galaktosidasy z Arthrobacter sp. C2-2 (cs)
skos:notation
  • RIV/60461373:22330/05:00015821!RIV06-MSM-22330___
http://linked.open...avai/riv/aktivita
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  • Z(MSM 223300006)
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  • 523233
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  • RIV/60461373:22330/05:00015821
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  • Hexameric Structure of Cold-Active beta-Galactosidase from Arthrobacter sp. C2-2 (en)
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  • [F2C2ADC5A64C]
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  • Dohnálek, Jan
  • Hašek, Jindřich
  • Lipovová, Petra
  • Skálová, Tereza
  • Spiwok, Vojtěch
  • Strnad, Hynek
  • Králová, Blanka
  • Petroková, Hana
  • Buchtelová, Eva
http://linked.open...n/vavai/riv/zamer
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  • 22330
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