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

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Standard

WrbA bridges bacterial flavodoxins and eukaryotic NAD(P)H:quinone oxidoreductases. / Carey, Jannette; Brynda, Jiri; Wolfová, Julie; Grandori, Rita; Gustavsson, Tobias; Ettrich, Rüdiger; Smatanová, Ivana Kutá.

In: Protein Science, Vol. 16, No. 10, 10.2007, p. 2301-5.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Carey, J, Brynda, J, Wolfová, J, Grandori, R, Gustavsson, T, Ettrich, R & Smatanová, IK 2007, 'WrbA bridges bacterial flavodoxins and eukaryotic NAD(P)H:quinone oxidoreductases', Protein Science, vol. 16, no. 10, pp. 2301-5. https://doi.org/10.1110/ps.073018907

APA

Carey, J., Brynda, J., Wolfová, J., Grandori, R., Gustavsson, T., Ettrich, R., & Smatanová, I. K. (2007). WrbA bridges bacterial flavodoxins and eukaryotic NAD(P)H:quinone oxidoreductases. Protein Science, 16(10), 2301-5. https://doi.org/10.1110/ps.073018907

Vancouver

Carey J, Brynda J, Wolfová J, Grandori R, Gustavsson T, Ettrich R et al. WrbA bridges bacterial flavodoxins and eukaryotic NAD(P)H:quinone oxidoreductases. Protein Science. 2007 Oct;16(10):2301-5. https://doi.org/10.1110/ps.073018907

Author

Carey, Jannette ; Brynda, Jiri ; Wolfová, Julie ; Grandori, Rita ; Gustavsson, Tobias ; Ettrich, Rüdiger ; Smatanová, Ivana Kutá. / WrbA bridges bacterial flavodoxins and eukaryotic NAD(P)H:quinone oxidoreductases. In: Protein Science. 2007 ; Vol. 16, No. 10. pp. 2301-5.

Bibtex

@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",

}

RIS

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

VL - 16

SP - 2301

EP - 2305

JO - Protein Science

JF - Protein Science

SN - 0961-8368

IS - 10

ER -

ID: 201046660