Crystallization and preliminary diffraction analysis of Escherichia coli WrbA in complex with its cofactor flavin mononucleotide

Julie Wolfová; Jeroen R. Mesters; Jiří Brynda; Rita Grandori; Antonino Natalello; Jannette Carey; Ivana Kutá Smatanová

doi:10.1107/S1744309107026103

Crystallization and preliminary diffraction analysis of Escherichia coli WrbA in complex with its cofactor flavin mononucleotide

Julie Wolfová, Jeroen R. Mesters, Jiří Brynda, Rita Grandori, Antonino Natalello, Jannette Carey, Ivana Kutá Smatanová

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

5 Scopus citations

Abstract

The flavoprotein WrbA from Escherichia coli is considered to be the prototype of a new family of multimeric flavodoxin-like proteins that are implicated in cell protection against oxidative stress. The present study is aimed at structural characterization of the E. coli protein with respect to its recently revealed oxidoreductase activity. Crystals of WrbA holoprotein in complex with the oxidized flavin cofactor (FMN) were obtained using standard vapour-diffusion techniques. Deep yellow tetragonal crystals obtained from differing crystallization conditions display different space groups and unit-cell parameters. X-ray crystal structures of the WrbA holoprotein have been determined to resolutions of 2.0 and 2.6 Å.

Original language	English (US)
Pages (from-to)	571-575
Number of pages	5
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	63
Issue number	7
DOIs	https://doi.org/10.1107/S1744309107026103
State	Published - Jun 15 2007

All Science Journal Classification (ASJC) codes

Condensed Matter Physics
Genetics
Biophysics
Structural Biology
Biochemistry

Keywords

Flavin cofactor
Flavoproteins

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10.1107/S1744309107026103

Cite this

Wolfová, J., Mesters, J. R., Brynda, J., Grandori, R., Natalello, A., Carey, J., & Kutá Smatanová, I. (2007). Crystallization and preliminary diffraction analysis of Escherichia coli WrbA in complex with its cofactor flavin mononucleotide. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 63(7), 571-575. https://doi.org/10.1107/S1744309107026103

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abstract = "The flavoprotein WrbA from Escherichia coli is considered to be the prototype of a new family of multimeric flavodoxin-like proteins that are implicated in cell protection against oxidative stress. The present study is aimed at structural characterization of the E. coli protein with respect to its recently revealed oxidoreductase activity. Crystals of WrbA holoprotein in complex with the oxidized flavin cofactor (FMN) were obtained using standard vapour-diffusion techniques. Deep yellow tetragonal crystals obtained from differing crystallization conditions display different space groups and unit-cell parameters. X-ray crystal structures of the WrbA holoprotein have been determined to resolutions of 2.0 and 2.6 {\AA}.",

keywords = "Flavin cofactor, Flavoproteins",

author = "Julie Wolfov{\'a} and Mesters, {Jeroen R.} and Ji{\v r}{\'i} Brynda and Rita Grandori and Antonino Natalello and Jannette Carey and {Kut{\'a} Smatanov{\'a}}, Ivana",

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Wolfová, J, Mesters, JR, Brynda, J, Grandori, R, Natalello, A, Carey, J & Kutá Smatanová, I 2007, 'Crystallization and preliminary diffraction analysis of Escherichia coli WrbA in complex with its cofactor flavin mononucleotide', Acta Crystallographica Section F: Structural Biology and Crystallization Communications, vol. 63, no. 7, pp. 571-575. https://doi.org/10.1107/S1744309107026103

Crystallization and preliminary diffraction analysis of Escherichia coli WrbA in complex with its cofactor flavin mononucleotide. / Wolfová, Julie; Mesters, Jeroen R.; Brynda, Jiří et al.
In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 63, No. 7, 15.06.2007, p. 571-575.

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

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T1 - Crystallization and preliminary diffraction analysis of Escherichia coli WrbA in complex with its cofactor flavin mononucleotide

AU - Wolfová, Julie

AU - Mesters, Jeroen R.

AU - Brynda, Jiří

AU - Grandori, Rita

AU - Natalello, Antonino

AU - Carey, Jannette

AU - Kutá Smatanová, Ivana

PY - 2007/6/15

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AB - The flavoprotein WrbA from Escherichia coli is considered to be the prototype of a new family of multimeric flavodoxin-like proteins that are implicated in cell protection against oxidative stress. The present study is aimed at structural characterization of the E. coli protein with respect to its recently revealed oxidoreductase activity. Crystals of WrbA holoprotein in complex with the oxidized flavin cofactor (FMN) were obtained using standard vapour-diffusion techniques. Deep yellow tetragonal crystals obtained from differing crystallization conditions display different space groups and unit-cell parameters. X-ray crystal structures of the WrbA holoprotein have been determined to resolutions of 2.0 and 2.6 Å.

KW - Flavin cofactor

KW - Flavoproteins

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Crystallization and preliminary diffraction analysis of Escherichia coli WrbA in complex with its cofactor flavin mononucleotide

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