About: Structural changes of tetrameric flavoprotein WrbA upon flavin binding

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About: Structural changes of tetrameric flavoprotein WrbA upon flavin binding Goto Sponge NotDistinct Permalink

An Entity of Type : http://linked.opendata.cz/ontology/domain/vavai/Vysledek, within Data Space : linked.opendata.cz associated with source document(s)

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rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
Description	Protein WrbA from Escherichia coli studied in this work represents a widely distributed family of tetrameric flavoenzymes [1, 2]. Using flavin mononucleotide (FMN) like monomeric flavodoxins that transfer single electrons to protein partners but forming multimers and carrying out two-electron reduction of quinones [3, 4] like the FAD-de - pend ent quinone oxidoreductases, WrbA was suggested to be a structural and functional linker between bacterial flavodoxins and eukaryotic NAD(P)H:quinone oxidoreductases [5]. Interesting changes in protein dynamics and multimerization state accompanying FMN binding were identified by biophysical spectral methods [6]. This was motivation for the comparative analysis of the FMN-bound WrbA structure (holoWrbA) and the FMN-free WrbA structure (apoWrbA), results of which are presented here. Protein WrbA from Escherichia coli studied in this work represents a widely distributed family of tetrameric flavoenzymes [1, 2]. Using flavin mononucleotide (FMN) like monomeric flavodoxins that transfer single electrons to protein partners but forming multimers and carrying out two-electron reduction of quinones [3, 4] like the FAD-de - pend ent quinone oxidoreductases, WrbA was suggested to be a structural and functional linker between bacterial flavodoxins and eukaryotic NAD(P)H:quinone oxidoreductases [5]. Interesting changes in protein dynamics and multimerization state accompanying FMN binding were identified by biophysical spectral methods [6]. This was motivation for the comparative analysis of the FMN-bound WrbA structure (holoWrbA) and the FMN-free WrbA structure (apoWrbA), results of which are presented here. (en)
Title	Structural changes of tetrameric flavoprotein WrbA upon flavin binding Structural changes of tetrameric flavoprotein WrbA upon flavin binding (en)
skos:prefLabel	Structural changes of tetrameric flavoprotein WrbA upon flavin binding Structural changes of tetrameric flavoprotein WrbA upon flavin binding (en)
skos:notation	RIV/60076658:12640/09:00010079!RIV10-MSM-12640___
http://linked.open...avai/riv/aktivita	P Z
http://linked.open...avai/riv/aktivity	P(LC06010), P(ME09016), Z(MSM6007665808)
http://linked.open...iv/cisloPeriodika	2a
http://linked.open...vai/riv/dodaniDat	2010
http://linked.open...aciTvurceVysledku	Wolfová, Julie Kutá-Smatanová, Ivana Brynda, Jiří Ettrich, Rüdiger
http://linked.open.../riv/druhVysledku	J - Článek v odborném periodiku
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Jihočeská univerzita v Českých Budějovicích / Ústav fyzikální biologie
http://linked.open...dnocenehoVysledku	344133
http://linked.open...ai/riv/idVysledku	RIV/60076658:12640/09:00010079
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	WrbA; flavoprotein; Escherichia coli; structural changes (en)
http://linked.open.../riv/klicoveSlovo	Escherichia coli structural changes flavoprotein WrbA
http://linked.open...odStatuVydavatele	CZ - Česká republika
http://linked.open...ontrolniKodProRIV	[31EDEC246E14]
http://linked.open...i/riv/nazevZdroje	Materials Structure
http://linked.open...in/vavai/riv/obor	BO
http://linked.open...ichTvurcuVysledku	4 (xsd:int)
http://linked.open...cetTvurcuVysledku	6 (xsd:int)
http://linked.open...vavai/riv/projekt	The role of WrbA protein in life Center of Biocatalysis and Biotransformation
http://linked.open...UplatneniVysledku	2009
http://linked.open...v/svazekPeriodika	16
http://linked.open...iv/tvurceVysledku	Brynda, Jiří Kutá-Smatanová, Ivana Carey, J. Ettrich, Rudiger Horst Wolfová, Julie Mesters, J. R.
http://linked.open...n/vavai/riv/zamer	Fyzikální biologie -nové přístupy v biologickém výzkumu
issn	1211-5894
number of pages	2 (xsd:int)
http://localhost/t...ganizacniJednotka	12640

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