Skip to main content

Lund University Publications

LUND UNIVERSITY LIBRARIES

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

Carey, Jannette ; Brynda, Jiri ; Wolfova, Julie ; Grandori, Rita ; Gustavsson, Tobias LU ; Ettrich, Ruediger and Smatanova, Ivana Kuta (2007) In Protein Science 16(10). p.2301-2305
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.
Please use this url to cite or link to this publication:
author
; ; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
vitamin K, menaquinone, peripheral membrane proteins, soluble quinones, membrane quinones, chemotherapeutics, shikimate
in
Protein Science
volume
16
issue
10
pages
2301 - 2305
publisher
The Protein Society
external identifiers
  • wos:000249692400022
  • scopus:34748879003
ISSN
1469-896X
DOI
10.1110/ps.073018907
language
English
LU publication?
yes
id
c9fee7fb-95f4-4758-86be-70bb263bf4ea (old id 655872)
date added to LUP
2016-04-01 12:35:24
date last changed
2022-01-27 07:11:47
@article{c9fee7fb-95f4-4758-86be-70bb263bf4ea,
  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.}},
  author       = {{Carey, Jannette and Brynda, Jiri and Wolfova, Julie and Grandori, Rita and Gustavsson, Tobias and Ettrich, Ruediger and Smatanova, Ivana Kuta}},
  issn         = {{1469-896X}},
  keywords     = {{vitamin K; menaquinone; peripheral membrane proteins; soluble quinones; membrane quinones; chemotherapeutics; shikimate}},
  language     = {{eng}},
  number       = {{10}},
  pages        = {{2301--2305}},
  publisher    = {{The Protein Society}},
  series       = {{Protein Science}},
  title        = {{WrbA bridges bacterial flavodoxins and eukaryotic NAD(P)H: quinone oxidoreductases}},
  url          = {{http://dx.doi.org/10.1110/ps.073018907}},
  doi          = {{10.1110/ps.073018907}},
  volume       = {{16}},
  year         = {{2007}},
}