TAILIEUCHUNG - Báo cáo khoa học: Solution structure and stability of the full-length excisionase from bacteriophage HK022

Heteronuclear high-resolution NMR spectroscopy was employed to determine the solution structure of the excisi-onase protein (Xis)from thek-like bacteriophage HK022 and to study its sequence-specificDNA interaction. Aswild-typeXiswas previously characterizedas a generallyunstable protein, abiologicallyactiveHK022Xismutantwithasingle amino acid substitutionCys28fiSerwas used in this work. This substitution has been shown to diminish the irreversi-bility of Xis denaturation and subsequent degradation, but does not affect the structural or thermodynamic properties of the protein, as evidenced by NMR and differential scan-ning calorimetry. . | Eur. J. Biochem. 270 4846-4858 2003 FEBS 2003 doi Solution structure and stability of the full-length excisionase from bacteriophage HK022 Vladimir V. Rogov1 2 Christian Liicke3 Lucia Muresanu1 Hans Wienk1 loana Kleinhaus1 Karla Werner1 Frank Lohr1 Primoz Pristovsek4 and Heinz Ruterjans1 1 Institute of Biophysical Chemistry . Goethe-University of Frankfurt Germany 2 Institute of Protein Research Pushchino Russia 3Max Planck Research Unit for Enzymology of Protein Folding Halle Germany 4National Institute of Chemistry Ljubljana Slovenia Heteronuclear high-resolution NMR spectroscopy was employed to determine the solution structure of the excisi-onase protein Xis from the k-like bacteriophage HK022 and to study its sequence-specific DNA interaction. As wildtype Xis was previously characterized as a generally unstable protein a biologically active HK022 Xis mutant with a single amino acid substitution Cys28 fi Ser was used in this work. This substitution has been shown to diminish the irreversibility of Xis denaturation and subsequent degradation but does not affect the structural or thermodynamic properties of the protein as evidenced by NMR and differential scanning calorimetry. The solution structure of HK022 Xis forms a compact highly ordered protein core with two well-defined a-helices residues 5-11 and 18-27 and five b-strands residues 2-4 30-31 35-36 41-44 and 48-49 . These data correlate well with 1H2O-2H2O exchange experiments and imply a different organization of the HK022 Xis secondary structure elements in comparison with the previously determined structure of the bacteriophage k excisionase. Superposition of both Xis structures indicates a better correspondence of the full-length HK022 Xis to the typical winged-helix DNA-binding motif as found for example in the DNA-binding domain of the Mu-phage repressor. Residues 51-72 which were not resolved in the k Xis do not show any regular structure in HK022 Xis and thus appear

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