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

Jannette Carey; Jiri Brynda; Julie Wolfová; Rita Grandori; Tobias Gustavsson; Rüdiger Ettrich; Ivana Kutá Smatanová

doi:10.1110/ps.073018907

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

Jannette Carey, Jiri Brynda, Julie Wolfová, Rita Grandori, Tobias Gustavsson, Rüdiger Ettrich, Ivana Kutá Smatanová

Research output: Contribution to journal › Article › peer-review

36 Scopus citations

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)
Pages (from-to)	2301-2305
Number of pages	5
Journal	Protein Science
Volume	16
Issue number	10
DOIs	https://doi.org/10.1110/ps.073018907
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

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10.1110/ps.073018907

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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.",

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AU - Carey, Jannette

AU - Brynda, Jiri

AU - Wolfová, Julie

AU - Grandori, Rita

AU - Gustavsson, Tobias

AU - Ettrich, Rüdiger

AU - Smatanová, Ivana Kutá

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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. Published by Cold Spring Harbor Laboratory Press.

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KW - Peripheral membrane proteins

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KW - Vitamin K

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

Abstract

All Science Journal Classification (ASJC) codes

Keywords

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