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Statements

Subject Item
n2:RIV%2F60076658%3A12640%2F08%3A00009373%21RIV09-MSM-12640___
rdf:type
skos:Concept n18:Vysledek
dcterms:description
Flavoprotein WrbA z E.coli reprezentuje novou rodinu multimerních proteinů podobných flavodoxinům zahrnutých v buněčné ochraně proti oxidativnímu stresu. V současnosti odhalenou NAD(P)H-dependentní chinon-oxidoreduktázovou aktivitu podněcuje určení krystalové struktury WrbA a následující výzkum strukturních rysů charakterizující novou rodinu redoxně aktivních proteinů. Dvě různé krystalové formy WrbA proteinu s navázaným kofaktorem FMN byly získány a následně určeny jejich krystalové struktury s rozlišením 2.6 and 2.0 Å. Z důvodu určit vliv FMN navázaného do aktivního místa, apoprotein WrbA (bez navázaného FMN) byl krystalizován a difrakční data naměřena do rozlišení 1.85 The flavoprotein WrbA from Escherichia coli represents a new family of multimeric flavodoxin-like proteins implicated in cell protection against oxidative stress. The recently revealed NAD(P)H-dependent quinone oxidoreductase activity stimulated determination of crystal structures of E. coli WrbA and the folowing search for structural features characterizing the new family of redox-active proteins. Two different crystal forms were obtained for E. coli WrbA in complex with its flavin cofactor (FMN) and the crystal structures were determined to resolutions of 2.6 and 2.0Å. In order to investigate influence of FMN binding on the protein structure, WrbA apoprotein (without FMN bound)was crystallized and the diffraction data were recorded to a resolution of 1.85 The flavoprotein WrbA from Escherichia coli represents a new family of multimeric flavodoxin-like proteins implicated in cell protection against oxidative stress. The recently revealed NAD(P)H-dependent quinone oxidoreductase activity stimulated determination of crystal structures of E. coli WrbA and the folowing search for structural features characterizing the new family of redox-active proteins. Two different crystal forms were obtained for E. coli WrbA in complex with its flavin cofactor (FMN) and the crystal structures were determined to resolutions of 2.6 and 2.0Å. In order to investigate influence of FMN binding on the protein structure, WrbA apoprotein (without FMN bound)was crystallized and the diffraction data were recorded to a resolution of 1.85
dcterms:title
Crystallographic study of Escherichia coli favoprotein WrbA, a new NAD(P)H-dependent guinine oxidoreductase Crystallographic study of Escherichia coli favoprotein WrbA, a new NAD(P)H-dependent guinine oxidoreductase Krystalografická studie flavoproteinu WrbA z E.coli, nové NAD(P)H-dependentní chinon-oxidoreduktasy
skos:prefLabel
Crystallographic study of Escherichia coli favoprotein WrbA, a new NAD(P)H-dependent guinine oxidoreductase Krystalografická studie flavoproteinu WrbA z E.coli, nové NAD(P)H-dependentní chinon-oxidoreduktasy Crystallographic study of Escherichia coli favoprotein WrbA, a new NAD(P)H-dependent guinine oxidoreductase
skos:notation
RIV/60076658:12640/08:00009373!RIV09-MSM-12640___
n4:aktivita
n7:Z n7:S n7:P
n4:aktivity
P(LC06010), P(ME 640), S, Z(MSM6007665808)
n4:cisloPeriodika
1
n4:dodaniDat
n8:2009
n4:domaciTvurceVysledku
n14:4694031 n14:4240642 n14:7774729
n4:druhVysledku
n19:J
n4:duvernostUdaju
n5:S
n4:entitaPredkladatele
n6:predkladatel
n4:idSjednocenehoVysledku
361647
n4:idVysledku
RIV/60076658:12640/08:00009373
n4:jazykVysledku
n12:eng
n4:klicovaSlova
Biological crystallography; flavoprotein; oxidoreductase activity; single crystal growth; X-ray diffraction
n4:klicoveSlovo
n10:Biological%20crystallography n10:oxidoreductase%20activity n10:X-ray%20diffraction n10:single%20crystal%20growth n10:flavoprotein
n4:kodStatuVydavatele
CZ - Česká republika
n4:kontrolniKodProRIV
[927C9068A132]
n4:nazevZdroje
Materials Structure
n4:obor
n11:BO
n4:pocetDomacichTvurcuVysledku
3
n4:pocetTvurcuVysledku
6
n4:projekt
n16:LC06010 n16:ME%20640
n4:rokUplatneniVysledku
n8:2008
n4:svazekPeriodika
15
n4:tvurceVysledku
Wolfová, Julie Carey, J. Kutá-Smatanová, Ivana Brynda, Jiří Mesters, J. R. Grandori, R.
n4:zamer
n17:MSM6007665808
s:issn
1211-5894
s:numberOfPages
3
n15:organizacniJednotka
12640