Journal of the Korean Magnetic Resonance Society (한국자기공명학회논문지)

Korean Magnetic Resonance Society (한국자기공명학회)
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Biochemical and Structural Characterization of HP1423 (Y1423_HELPY) from Helicobacter pylori

  • Kim, Ji-Hun (Research Inst. of Pharmaceutical Sciences, College of Pharmacy, Seoul National University) ;
  • Lee, Ki-Young (Research Inst. of Pharmaceutical Sciences, College of Pharmacy, Seoul National University) ;
  • Park, Sung-Jean (Gachon University of Medicine and Science) ;
  • Lee, Bong-Jin (Research Inst. of Pharmaceutical Sciences, College of Pharmacy, Seoul National University)
  • Received : 2010.04.21
  • Published : 2010.06.20
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Abstract

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.

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