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

VAR2CSA team

33 Citations (Scopus)

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.

Original language	English
Journal	Protein Science
Volume	16
Issue number	10
Pages (from-to)	2301-5
Number of pages	5
ISSN	0961-8368
DOIs	https://doi.org/10.1110/ps.073018907
Publication status	Published - Oct 2007

Keywords

Binding Sites
DNA-Binding Proteins/chemistry
Escherichia coli Proteins/chemistry
Flavodoxin/chemistry
Models, Molecular
NAD(P)H Dehydrogenase (Quinone)/chemistry
Protein Folding
Repressor Proteins/chemistry

Access to Document

10.1110/ps.073018907

Cite this

@article{18c4fdfa108e41c0ac565986317e7f43,

title = "WrbA bridges bacterial flavodoxins and eukaryotic NAD(P)H:quinone oxidoreductases",

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.",

keywords = "Binding Sites, DNA-Binding Proteins/chemistry, Escherichia coli Proteins/chemistry, Flavodoxin/chemistry, Models, Molecular, NAD(P)H Dehydrogenase (Quinone)/chemistry, Protein Folding, Repressor Proteins/chemistry",

author = "Jannette Carey and Jiri Brynda and Julie Wolfov{\'a} and Rita Grandori and Tobias Gustavsson and R{\"u}diger Ettrich and Smatanov{\'a}, {Ivana Kut{\'a}}",

year = "2007",

month = oct,

doi = "10.1110/ps.073018907",

language = "English",

volume = "16",

pages = "2301--5",

journal = "Protein Science",

issn = "0961-8368",

publisher = "Wiley-Blackwell",

number = "10",

}

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 -

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

Abstract

Keywords

Access to Document

Fingerprint

Cite this