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*

*Korrespondierende/r Autor/-in für diese Arbeit
3 Zitate (Scopus)

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.

OriginalspracheEnglisch
ZeitschriftActa Crystallographica Section F: Structural Biology and Crystallization Communications
Jahrgang63
Ausgabenummer7
Seiten (von - bis)571-575
Seitenumfang5
ISSN1744-3091
DOIs
PublikationsstatusVeröffentlicht - 15.06.2007

Strategische Forschungsbereiche und Zentren

  • Forschungsschwerpunkt: Infektion und Entzündung - Zentrum für Infektions- und Entzündungsforschung Lübeck (ZIEL)

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