Title | WrbA bridges bacterial flavodoxins and eukaryotic NAD(P)H:quinone oxidoreductases. |
Publication Type | Journal Article |
Year of Publication | 2007 |
Authors | Carey, J, Brynda, J, Wolfová, J, Grandori, R, Gustavsson, T, Ettrich, R, Smatanová, IKutá |
Journal | Protein Sci |
Volume | 16 |
Issue | 10 |
Pagination | 2301-5 |
Date Published | 2007 Oct |
ISSN | 0961-8368 |
Keywords | Binding 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> |
DOI | 10.1110/ps.073018907 |
Alternate Journal | Protein Sci |
PubMed ID | 17893367 |
PubMed Central ID | PMC2204128 |