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Statements

Subject Item
n2:RIV%2F60461373%3A22330%2F05%3A00019974%21RIV09-MSM-22330___
rdf:type
n3:Vysledek skos:Concept
dcterms:description
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 Chladově-aktivní beta-galaktosidasa z Arthrobacter sp. C2-2 tvoří kompaktní hexamery o hmotnosti 660 kDa; krystalová struktura s rozlišením 1.9 A. 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
dcterms: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. Cold-Active beta-Galactosidase from Arthrobacter sp. C2-2 Forms Compact 660 kDa Hexamers; Crystal Structure at 1.9 A Resolution.
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. Cold-Active beta-Galactosidase from Arthrobacter sp. C2-2 Forms Compact 660 kDa Hexamers; Crystal Structure at 1.9 A Resolution.
skos:notation
RIV/60461373:22330/05:00019974!RIV09-MSM-22330___
n5:aktivita
n12:P n12:Z
n5:aktivity
P(GA204/02/0843), P(KJB500500512), Z(AV0Z40500505), Z(MSM 223300006)
n5:cisloPeriodika
2
n5:dodaniDat
n18:2009
n5:domaciTvurceVysledku
n13:9836861 n13:4654730 n13:1473190 n13:3105849
n5:druhVysledku
n10:J
n5:duvernostUdaju
n17:S
n5:entitaPredkladatele
n15:predkladatel
n5:idSjednocenehoVysledku
515660
n5:idVysledku
RIV/60461373:22330/05:00019974
n5:jazykVysledku
n6:eng
n5:klicovaSlova
glycosyl hydrolase; beta-galactosidase; cold-active; psychrotrophic; crystal structure
n5:klicoveSlovo
n8:psychrotrophic n8:beta-galactosidase n8:glycosyl%20hydrolase n8:cold-active n8:crystal%20structure
n5:kodStatuVydavatele
GB - Spojené království Velké Británie a Severního Irska
n5:kontrolniKodProRIV
[FB76CFD7D9AC]
n5:nazevZdroje
Journal of Molecular Biology
n5:obor
n14:EB
n5:pocetDomacichTvurcuVysledku
4
n5:pocetTvurcuVysledku
10
n5:projekt
n9:GA204%2F02%2F0843 n9:KJB500500512
n5:rokUplatneniVysledku
n18:2005
n5:svazekPeriodika
353
n5:tvurceVysledku
Lipovová, Petra Dušková, Jarmila Dohnálek, Jan Spiwok, Vojtěch Vondráčková, E. Strnad, Hynek Hašek, Jindřich Králová, Blanka Petroková, Hana Skálová, Tereza
n5:wos
000232505600007
n5:zamer
n19:MSM%20223300006 n19:AV0Z40500505
s:issn
0022-2836
s:numberOfPages
13
n16:organizacniJednotka
22330