WrbA bridges bacterial flavodoxins and eukaryotic NAD(P)H:quinone oxidoreductases
Research output: Contribution to journal › Journal article › Research › peer-review
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.
Original language | English |
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Journal | Protein Science |
Volume | 16 |
Issue number | 10 |
Pages (from-to) | 2301-5 |
Number of pages | 5 |
ISSN | 0961-8368 |
DOIs | |
Publication status | Published - Oct 2007 |
- Binding Sites, DNA-Binding Proteins/chemistry, Escherichia coli Proteins/chemistry, Flavodoxin/chemistry, Models, Molecular, NAD(P)H Dehydrogenase (Quinone)/chemistry, Protein Folding, Repressor Proteins/chemistry
Research areas
ID: 201046660