| Autor: |
Carey, Jannette, Brynda, Jiri, Wolfová, Julie, Grandori, Rita, Gustavsson, Tobias, Ettrich, Rüdiger, Smatanová, Ivana Kutá |
| Zdroj: |
Protein Science: A Publication of the Protein Society; 2007, Vol. 16 Issue 10, p2301-2305, 5p |
| Abstrakt: |
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. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
|
Plný text