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

TY - JOUR

T1 - WrbA bridges bacterial flavodoxins and eukaryotic NAD(P)H:quinone oxidoreductases

AU - Carey, Jannette

AU - Brynda, Jiri

AU - Wolfová, Julie

AU - Grandori, Rita

AU - Gustavsson, Tobias

AU - Ettrich, Rüdiger

AU - Smatanová, Ivana Kutá

PY - 2007/10

Y1 - 2007/10

N2 - 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.

AB - 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.

KW - Binding Sites

KW - DNA-Binding Proteins/chemistry

KW - Escherichia coli Proteins/chemistry

KW - Flavodoxin/chemistry

KW - Models, Molecular

KW - NAD(P)H Dehydrogenase (Quinone)/chemistry

KW - Protein Folding

KW - Repressor Proteins/chemistry

U2 - 10.1110/ps.073018907

DO - 10.1110/ps.073018907

M3 - Journal article

C2 - 17893367

SN - 0961-8368

VL - 16

SP - 2301

EP - 2305

JO - Protein Science

JF - Protein Science

IS - 10

ER -