Genomes and Genes
Gene Symbol: wrbA
Description: NAD(P)H:quinone oxidoreductase
Alias: ECK0995, JW0989
Species: Escherichia coli str. K-12 substr. MG1655
- Kirkpatrick C, Maurer L, Oyelakin N, Yoncheva Y, Maurer R, Slonczewski J. Acetate and formate stress: opposite responses in the proteome of Escherichia coli. J Bacteriol. 2001;183:6466-77 pubmed
- Grandori R, Carey J. Six new candidate members of the alpha/beta twisted open-sheet family detected by sequence similarity to flavodoxin. Protein Sci. 1994;3:2185-93 pubmedStrong sequence similarity has been reported among WrbA (the Trp repressor-binding protein of Escherichia coli); Ycp4, a protein of unknown function from the budding yeast Saccharomyces cerevisiae; P25, the pap1-dependent protein of the ..
- Gorman J, Shapiro L. Crystal structures of the tryptophan repressor binding protein WrbA and complexes with flavin mononucleotide. Protein Sci. 2005;14:3004-12 pubmed publisherThe tryptophan repressor binding protein WrbA binds to the tryptophan repressor protein TrpR. Although the biological role of WrbA remains unclear, it has been proposed to function in enhancing the stability of TrpR-DNA complexes...
- Nöll G, Kozma E, Grandori R, Carey J, Schödl T, Hauska G, et al. Spectroelectrochemical investigation of a flavoprotein with a flavin-modified gold electrode. Langmuir. 2006;22:2378-83 pubmed..was successfully applied to the electrochemical and spectroelectrochemical investigation of the flavoprotein WrbA from Escherichia coli that shows some structural similarities to flavodoxins...
- Patridge E, Ferry J. WrbA from Escherichia coli and Archaeoglobus fulgidus is an NAD(P)H:quinone oxidoreductase. J Bacteriol. 2006;188:3498-506 pubmed publisherb>WrbA (tryptophan [W] repressor-binding protein) was discovered in Escherichia coli, where it was proposed to play a role in regulation of the tryptophan operon; however, this has been put in question, leaving the function unknown...
- Liu X, De Wulf P. Probing the ArcA-P modulon of Escherichia coli by whole genome transcriptional analysis and sequence recognition profiling. J Biol Chem. 2004;279:12588-97 pubmed..A conservative but reasonable assessment is that the Arc pathway recruits 100-150 operons to mediate a role in cellular adaptation that is more extensive than hitherto anticipated. ..
- Wolfova J, Mesters J, Brynda J, Grandori R, Natalello A, Carey J, et al. Crystallization and preliminary diffraction analysis of Escherichia coli WrbA in complex with its cofactor flavin mononucleotide. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007;63:571-5 pubmedThe 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...
- Andrade S, Patridge E, Ferry J, Einsle O. Crystal structure of the NADH:quinone oxidoreductase WrbA from Escherichia coli. J Bacteriol. 2007;189:9101-7 pubmedThe flavoprotein WrbA, originally described as a tryptophan (W) repressor-binding protein in Escherichia coli, has recently been shown to exhibit the enzymatic activity of a NADH:quinone oxidoreductase...
- Tjaden B, Goodwin S, Opdyke J, Guillier M, Fu D, Gottesman S, et al. Target prediction for small, noncoding RNAs in bacteria. Nucleic Acids Res. 2006;34:2791-802 pubmed..Our results show that TargetRNA is a useful tool for finding mRNA targets of sRNAs, although its rate of success varies between sRNAs. ..
- Loewen P, Hu B, Strutinsky J, Sparling R. Regulation in the rpoS regulon of Escherichia coli. Can J Microbiol. 1998;44:707-17 pubmed..The activity of sigma s may also be modulated by trehalose and glutamate, which activate holoenzyme formation and promote holoenzyme binding to certain promoters. ..
- Wolfova J, Smatanova I, Brynda J, Mesters J, Lapkouski M, Kuty M, et al. Structural organization of WrbA in apo- and holoprotein crystals. Biochim Biophys Acta. 2009;1794:1288-98 pubmed publisherTwo previously reported holoprotein crystal forms of the flavodoxin-like E. coli protein WrbA, diffracting to 2.6 and 2.0 A resolution, and new crystals of WrbA apoprotein diffracting to 1...