@article{2633,
  keywords = {Repressor Proteins, Binding Sites, Models, Molecular, Escherichia coli Proteins, Protein Folding, DNA-Binding Proteins, Flavodoxin, NAD(P)H Dehydrogenase (Quinone)},
  author = {Jannette Carey and Jiri Brynda and Julie Wolfov{\'a} and Rita Grandori and Tobias Gustavsson and R{\"u}diger Ettrich and Ivana Smatanov{\'a}},
  title = {WrbA bridges bacterial flavodoxins and eukaryotic NAD(P)H:quinone oxidoreductases.},
  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> },
  year = {2007},
  journal = {Protein Sci},
  volume = {16},
  pages = {2301-5},
  month = {2007 Oct},
  issn = {0961-8368},
  doi = {10.1110/ps.073018907},
  language = {eng},
}