Crystallization and preliminary diffraction analysis of Escherichia coli WrbA in complex with its cofactor flavin mononucleotide
| Autor: | Ivana Kuta Smatanova, Jannette Carey, J. Wolfova, Jiří Brynda, Rita Grandori, Antonino Natalello, Jeroen R. Mesters |
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| Přispěvatelé: | Wolfova, J, Mesters, J, Brynda, J, Grandori, R, Natalello, A, Carey, J, Smatanova, I |
| Jazyk: | angličtina |
| Rok vydání: | 2007 |
| Předmět: |
crystallization of complexe
Biocrystallization Stereochemistry Flavin Mononucleotide Biophysics Flavoprotein Flavin mononucleotide flavin cofactor Flavin group medicine.disease_cause Crystallography X-Ray Biochemistry environment and public health Cofactor law.invention chemistry.chemical_compound Structural Biology law Oxidoreductase flavoprotein Genetics medicine Escherichia coli Crystallization chemistry.chemical_classification biology integumentary system Chemistry Escherichia coli Proteins Condensed Matter Physics humanities X-ray diffraction DNA-Binding Proteins Repressor Proteins Crystallography enzymes and coenzymes (carbohydrates) Crystallization Communications biology.protein bacteria |
| Popis: | 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 angstrom |
| Databáze: | OpenAIRE |
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