Open AccessCrystallization and preliminary diffraction analysis of Escherichia coli WrbA in complex with its cofactor flavin mononucleotide
Author(s) -
Wolfová Julie,
Mesters Jeroen R.,
Brynda Jiří,
Grandori Rita,
Natalello Antonino,
Carey Jannette,
Kutá Smatanová Ivana
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107026103
Subject(s) - flavin mononucleotide , flavoprotein , cofactor , crystallization , flavin group , crystallography , escherichia coli , flavodoxin , chemistry , tetragonal crystal system , oxidoreductase , flavin adenine dinucleotide , stereochemistry , crystal structure , biochemistry , ferredoxin , enzyme , organic chemistry , gene
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.