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Protein Science (2007), 16:2301-2305. Published by Cold Spring Harbor Laboratory Press. Copyright © 2007 The Protein Society
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FOR THE RECORD

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

Jannette Carey1, Jiri Brynda2,3,4, Julie Wolfová4,5, Rita Grandori6, Tobias Gustavsson7, Rüdiger Ettrich4,5, and Ivana Kutá Smatanová4,5

1 Chemistry Department, Princeton University, New Jersey 08544-1009, USA
2 Institute of Molecular Genetics, Academy of Sciences of the Czech Republic, CZ-166 10 Prague 6, Czech Republic
3 Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, CZ-166 10 Prague 6, Czech Republic
4 Institute of Physical Biology, University of South Bohemia, CZ-373 33 Nové Hrady, Czech Republic
5 Institute of Systems Biology and Ecology, Academy of Sciences of the Czech Republic, CZ-373 33 Nové Hrady, Czech Republic
6 Department of Biotechnology and Biosciences, University of Milano–Bicocca, 20126 Milan, Italy
7 Biochemistry Department, Lund University, Chemical Center, S-221 00 Lund, Sweden

(RECEIVED May 23, 2007; FINAL REVISION July 13, 2007; ACCEPTED July 13, 2007)

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.

Keywords: soluble quinones; membrane quinones; peripheral membrane proteins; menaquinone; vitamin K; shikimate; chemotherapeutics


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