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

Jannette Carey, Jiri Brynda, Julie Wolfová, Rita Grandori, Tobias Gustavsson, Rüdiger Ettrich, Ivana Kutá Smatanová

Research output: Contribution to journalArticle

30 Scopus citations

Abstract

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. Published by Cold Spring Harbor Laboratory Press.

Original languageEnglish (US)
Pages (from-to)2301-2305
Number of pages5
JournalProtein Science
Volume16
Issue number10
DOIs
StatePublished - Oct 2007

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

Keywords

  • Chemotherapeutics
  • Membrane quinones
  • Menaquinone
  • Peripheral membrane proteins
  • Shikimate
  • Soluble quinones
  • Vitamin K

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    Carey, J., Brynda, J., Wolfová, J., Grandori, R., Gustavsson, T., Ettrich, R., & Smatanová, I. K. (2007). WrbA bridges bacterial flavodoxins and eukaryotic NAD(P)H:quinone oxidoreductases. Protein Science, 16(10), 2301-2305. https://doi.org/10.1110/ps.073018907