Altered active site flexibility and a structural metal-binding site in eukaryotic dUTPase: kinetic characterization, folding, and crystallographic studies of the homotrimeric Drosophila enzyme

dUTPase is responsible for preventive DNA repair via exclusion of uracil. Developmental regulation of the Drosophila enzyme is suggested to be involved in thymine-less apoptosis. Here we show that in addition to conserved dUTPase sequence motifs, the gene of Drosophila enzyme codes for a unique Ala-...

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Veröffentlicht in:	The Journal of biological chemistry 2004-04, Vol.279 (17), p.17932-17944
Hauptverfasser:	Kovári, Júlia, Barabás, Orsolya, Takács, Enikõ, Békési, Angéla, Dubrovay, Zsófia, Pongrácz, Veronika, Zagyva, Imre, Imre, Timea, Szabó, Pál, Vértessy, Beáta G
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Motifs Amino Acid Sequence Animals Apoptosis Binding Sites Calorimetry Catalysis Chromatography, Thin Layer Circular Dichroism Crystallography, X-Ray Dimerization DNA Repair Drosophila melanogaster - enzymology Electrophoresis, Polyacrylamide Gel Escherichia coli - metabolism Genetic Vectors Ions Kinetics Light Magnesium - chemistry Mass Spectrometry Models, Genetic Models, Molecular Molecular Sequence Data Plasmids - metabolism Protein Binding Protein Conformation Protein Denaturation Protein Folding Protein Structure, Tertiary Pyrophosphatases - chemistry Recombinant Proteins - chemistry Scattering, Radiation Spectrophotometry Substrate Specificity Temperature Thermodynamics Thymine - chemistry Trypsin - chemistry X-Rays
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