WrbA bridges bacterial flavodoxins and eukaryotic NAD(P)H:quinone oxidoreductases.

TitleWrbA bridges bacterial flavodoxins and eukaryotic NAD(P)H:quinone oxidoreductases.
Publication TypeJournal Article
Year of Publication2007
AuthorsCarey, J, Brynda, J, Wolfová, J, Grandori, R, Gustavsson, T, Ettrich, R, Smatanová, IKutá
JournalProtein Sci
Volume16
Issue10
Pagination2301-5
Date Published2007 Oct
ISSN0961-8368
KeywordsBinding Sites, DNA-Binding Proteins, Escherichia coli Proteins, Flavodoxin, Models, Molecular, NAD(P)H Dehydrogenase (Quinone), Protein Folding, Repressor Proteins
Abstract

<p>The crystal structure of the flavodoxin-like protein WrbA with oxidized FMN bound reveals a close relationship to mammalian NAD(P)H:quinone oxidoreductase, Nqo1. Structural comparison of WrbA, flavodoxin, and Nqo1 indicates how the twisted open-sheet fold of flavodoxins is elaborated to form multimers that extend catalytic function from one-electron transfer between protein partners using FMN to two-electron reduction of xenobiotics using FAD. The structure suggests a novel physiological role for WrbA and Nqo1.</p>

DOI10.1110/ps.073018907
Alternate JournalProtein Sci.
PubMed ID17893367
PubMed Central IDPMC2204128