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.

Carey, J., Brynda, J., Wolfová, J., Grandori, R., Gustavsson, T., Ettrich, R., et al. (2007). WrbA bridges bacterial flavodoxins and eukaryotic NAD(P)H:quinone oxidoreductases. PROTEIN SCIENCE, 16(10), 2301-2305 [10.1110/ps.073018907].

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

GRANDORI, RITA;
2007

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.
Articolo in rivista - Articolo scientifico
soluble quinones; membrane quinones; peripheral membrane proteins; menaquinone; vitamin K; shikimate; chemotherapeutics.
English
ott-2007
16
10
2301
2305
none
Carey, J., Brynda, J., Wolfová, J., Grandori, R., Gustavsson, T., Ettrich, R., et al. (2007). WrbA bridges bacterial flavodoxins and eukaryotic NAD(P)H:quinone oxidoreductases. PROTEIN SCIENCE, 16(10), 2301-2305 [10.1110/ps.073018907].
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/10281/403
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