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 journalArticle

3 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 languageEnglish (US)
Pages (from-to)571-575
Number of pages5
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume63
Issue number7
DOIs
StatePublished - Jun 15 2007

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

Keywords

  • Flavin cofactor
  • Flavoproteins

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