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http://dx.doi.org/10.6564/JKMRS.2010.14.1.045

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)
Publication Information
Journal of the Korean Magnetic Resonance Society / v.14, no.1, 2010 , pp. 45-54 More about this Journal
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.
Keywords
Helicobacter pylori; NMR, HP1423; Backbone assignment; Secondary structure;
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