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 language | English (US) |
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Pages (from-to) | 2301-2305 |
Number of pages | 5 |
Journal | Protein Science |
Volume | 16 |
Issue number | 10 |
DOIs | |
State | Published - Oct 2007 |
All Science Journal Classification (ASJC) codes
- Molecular Biology
- Biochemistry
Keywords
- Chemotherapeutics
- Membrane quinones
- Menaquinone
- Peripheral membrane proteins
- Shikimate
- Soluble quinones
- Vitamin K