• Title/Summary/Keyword: NMR, HP1423

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Biochemical and Structural Characterization of HP1423 (Y1423_HELPY) from Helicobacter pylori

  • Kim, Ji-Hun;Lee, Ki-Young;Park, Sung-Jean;Lee, Bong-Jin
    • Journal of the Korean Magnetic Resonance Society
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    • v.14 no.1
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    • pp.45-54
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    • 2010
  • HP1423 (Y1423_HELPY) is a conserved hypothetical protein from H. pylori strain 26695. However, Sequence Blast result indicates that HP1423 belongs to S4 (PF01479) superfamily. According to Pfam database, the S4 domain is a small domain consisting of 60-65 amino acid residues, that probably mediates binding to RNA. In this study, we report the sequence-specific backbone resonance assignment of HP1423, which has 84 amino acid residues. We could assign unambiguously about 88% of all $^{1}H_{N}$, $^{15}N$, $^{13}C_{\alpha}$, $^{13}C_{\beta}$ and $^{13}C=O$ resonances. We could not detect the resonances from residues 15-20, and disappearance of these peaks seems to be related with the intermediate-conformational exchange. These assigned NMR peaks of HP1423 can be used for studying the role of protein dynamics in millisecond timescale, and Protein-RNA binding.