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

38 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

Access to Document

10.1110/ps.073018907

Cite this

@article{be58a18c8c864b88b883ca50e21113d6,

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. Published by Cold Spring Harbor Laboratory Press.",

keywords = "Chemotherapeutics, Membrane quinones, Menaquinone, Peripheral membrane proteins, Shikimate, Soluble quinones, Vitamin K",

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 (US)",

volume = "16",

pages = "2301--2305",

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. Published by Cold Spring Harbor Laboratory Press.

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.

KW - Chemotherapeutics

KW - Membrane quinones

KW - Menaquinone

KW - Peripheral membrane proteins

KW - Shikimate

KW - Soluble quinones

KW - Vitamin K

UR - http://www.scopus.com/inward/record.url?scp=34748879003&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=34748879003&partnerID=8YFLogxK

U2 - 10.1110/ps.073018907

DO - 10.1110/ps.073018907

M3 - Article

C2 - 17893367

AN - SCOPUS:34748879003

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

All Science Journal Classification (ASJC) codes

Keywords

Access to Document

Other files and links

Fingerprint

Cite this