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| rdf:type
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| Description
| - Chladově-aktivní beta-galaktosidasa z Arthrobacter sp. C2-2 tvoří kompaktní hexamery o hmotnosti 660 kDa; krystalová struktura s rozlišením 1.9 A. (cs)
- The X-ray structure of cold-active beta-galactosidase (isoenzyme C-2-2-1) from an Antarctic bacterium Arthrobacter sp. C2-2 was solved at 1.9A resolution. The enzyme forms 660 kDa hexamers with active sites opened to the central cavity of the hexamer and connected by eight channels with exterior solvent. To our best knowledge, this is the first cold-active beta-galactosidase with known structure and also the first known beta-galactosidase structure in the form of compact hexamers. The hexamer organization regulates access of substrates and ligands to six active sites and this unique packing, present also in solution, raises questions about its purpose and function. This enzyme belongs to glycosyl hydrolase family 2, similarly to Escherichia coli beta-galactosidase, forming tetramers necessary for its enzymatic function. However, we discovered significant differences between these two enzymes affecting the ability of tetramer/hexamer formation and complementation of the active site. This structure reve
- The X-ray structure of cold-active beta-galactosidase (isoenzyme C-2-2-1) from an Antarctic bacterium Arthrobacter sp. C2-2 was solved at 1.9A resolution. The enzyme forms 660 kDa hexamers with active sites opened to the central cavity of the hexamer and connected by eight channels with exterior solvent. To our best knowledge, this is the first cold-active beta-galactosidase with known structure and also the first known beta-galactosidase structure in the form of compact hexamers. The hexamer organization regulates access of substrates and ligands to six active sites and this unique packing, present also in solution, raises questions about its purpose and function. This enzyme belongs to glycosyl hydrolase family 2, similarly to Escherichia coli beta-galactosidase, forming tetramers necessary for its enzymatic function. However, we discovered significant differences between these two enzymes affecting the ability of tetramer/hexamer formation and complementation of the active site. This structure reve (en)
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| Title
| - Cold-Active beta-Galactosidase from Arthrobacter sp. C2-2 Forms Compact 660 kDa Hexamers; Crystal Structure at 1.9 A Resolution.
- Chladově-aktivní beta-galaktosidasa z Arthrobacter sp. C2-2 tvoří kompaktní hexamery o hmotnosti 660 kDa; krystalová struktura s rozlišením 1.9 A. (cs)
- Cold-Active beta-Galactosidase from Arthrobacter sp. C2-2 Forms Compact 660 kDa Hexamers; Crystal Structure at 1.9 A Resolution. (en)
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| skos:prefLabel
| - Cold-Active beta-Galactosidase from Arthrobacter sp. C2-2 Forms Compact 660 kDa Hexamers; Crystal Structure at 1.9 A Resolution.
- Chladově-aktivní beta-galaktosidasa z Arthrobacter sp. C2-2 tvoří kompaktní hexamery o hmotnosti 660 kDa; krystalová struktura s rozlišením 1.9 A. (cs)
- Cold-Active beta-Galactosidase from Arthrobacter sp. C2-2 Forms Compact 660 kDa Hexamers; Crystal Structure at 1.9 A Resolution. (en)
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| skos:notation
| - RIV/60461373:22330/05:00019974!RIV09-MSM-22330___
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| http://linked.open...avai/riv/aktivita
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| http://linked.open...avai/riv/aktivity
| - P(GA204/02/0843), P(KJB500500512), Z(AV0Z40500505), Z(MSM 223300006)
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| http://linked.open...iv/cisloPeriodika
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| http://linked.open...vai/riv/dodaniDat
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| http://linked.open...aciTvurceVysledku
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| http://linked.open.../riv/druhVysledku
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| http://linked.open...iv/duvernostUdaju
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| http://linked.open...titaPredkladatele
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| http://linked.open...dnocenehoVysledku
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| http://linked.open...ai/riv/idVysledku
| - RIV/60461373:22330/05:00019974
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| http://linked.open...riv/jazykVysledku
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| http://linked.open.../riv/klicovaSlova
| - glycosyl hydrolase; beta-galactosidase; cold-active; psychrotrophic; crystal structure (en)
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| http://linked.open.../riv/klicoveSlovo
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| http://linked.open...odStatuVydavatele
| - GB - Spojené království Velké Británie a Severního Irska
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| http://linked.open...ontrolniKodProRIV
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| http://linked.open...i/riv/nazevZdroje
| - Journal of Molecular Biology
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| http://linked.open...in/vavai/riv/obor
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| http://linked.open...ichTvurcuVysledku
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| http://linked.open...cetTvurcuVysledku
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| http://linked.open...vavai/riv/projekt
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| http://linked.open...UplatneniVysledku
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| http://linked.open...v/svazekPeriodika
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| http://linked.open...iv/tvurceVysledku
| - Dohnálek, Jan
- Dušková, Jarmila
- Hašek, Jindřich
- Lipovová, Petra
- Skálová, Tereza
- Spiwok, Vojtěch
- Strnad, Hynek
- Králová, Blanka
- Petroková, Hana
- Vondráčková, E.
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| http://linked.open...ain/vavai/riv/wos
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| http://linked.open...n/vavai/riv/zamer
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| issn
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| number of pages
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| http://localhost/t...ganizacniJednotka
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| is http://linked.open...avai/riv/vysledek
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