Crystallization and preliminary diffraction analysis of Escherichia coli WrbA in complex with its cofactor flavin mononucleotide
- Institute of Physical Biology, University of South Bohemia České Budějovice, Zámek 136, CZ-373 33 Nové Hrady (Czech Republic)
- Institute of Biochemistry, Center for Structural and Cell Biology in Medicine, University of Lübeck, Ratzeburger Allee 160, 23538 Lübeck (Germany)
- Department of Biotechnology and Biosciences, University of Milano-Bicocca, Piazza della Scienza 2, 20126 Milan (Italy)
- Chemistry Department, Princeton University, Washington Road and William Street, Princeton, NJ 08544-1009 (United States)
E. coli WrbA, the founding member of a novel flavoprotein family, was crystallized in complex with its physiological cofactor. Preliminary diffraction analysis is reported. 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.
- OSTI ID:
- 22360363
- Journal Information:
- Acta Crystallographica. Section F, Vol. 63, Issue Pt 7; Other Information: PMCID: PMC2335133; PMID: 17620713; PUBLISHER-ID: gj5020; OAI: oai:pubmedcentral.nih.gov:2335133; Copyright (c) International Union of Crystallography 2007; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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