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  • 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
http://linked.open...avai/riv/aktivity
  • P(LC06010), P(ME09016), Z(MSM6007665808)
http://linked.open...iv/cisloPeriodika
  • 2a
http://linked.open...vai/riv/dodaniDat
http://linked.open...aciTvurceVysledku
http://linked.open.../riv/druhVysledku
http://linked.open...iv/duvernostUdaju
http://linked.open...titaPredkladatele
http://linked.open...dnocenehoVysledku
  • 344133
http://linked.open...ai/riv/idVysledku
  • RIV/60076658:12640/09:00010079
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • WrbA; flavoprotein; Escherichia coli; structural changes (en)
http://linked.open.../riv/klicoveSlovo
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
http://linked.open...ichTvurcuVysledku
http://linked.open...cetTvurcuVysledku
http://linked.open...vavai/riv/projekt
http://linked.open...UplatneniVysledku
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
issn
  • 1211-5894
number of pages
http://localhost/t...ganizacniJednotka
  • 12640
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