Structural changes of tetrameric flavoprotein WrbA upon flavin binding

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12640%2F09%3A00010079" target="_blank" >RIV/60076658:12640/09:00010079 - isvavai.cz</a>
Result on the web
—
DOI - Digital Object Identifier
—

Result language
angličtina
Original language name
Structural changes of tetrameric flavoprotein WrbA upon flavin binding
Original language 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 formingmultimers 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.
Czech name
—
Czech description
—

Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
BO - Biophysics
OECD FORD branch
—

Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)

Publication year
2009
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Similar results(10)