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HP0902 from Helicobacter pylori is a thermostable, dimeric protein belonging to an all-β topology of the cupin superfamily

  • Sim, Dae-Won (Department of Biotechnology, College of Biomedical and Health Science, Konkuk University) ;
  • Lee, Yoo-Sup (Department of Biotechnology, College of Biomedical and Health Science, Konkuk University) ;
  • Kim, Ji-Hun (Reseearch Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University) ;
  • Seo, Min-Duk (Reseearch Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University) ;
  • Lee, Bong-Jin (Reseearch Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University) ;
  • Won, Hyung-Sik (Department of Biotechnology, College of Biomedical and Health Science, Konkuk University)
  • Published : 2009.06.30
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Abstract

Here, we report the first biochemical and structural characterization of the hypothetical protein HP0902 from Helicobacter pylori, in terms of structural genomics. Gel-permeation chromatography and dynamic light scattering indicated that the protein behaves as a dimer in solution. Circular dichroism spectroscopy showed that HP0902 primarily adopts a $\beta$-structure and the protein was highly thermostable with a denaturing temperature higher than $70^{\circ}C$. Finally, the backbone NMR assignments were obtained on the [$^{13}C,^{15}N$]HP0902 and the secondary structure was determined using the chemical shift data. Additionally, the local flexibility was assessed via a heteronuclear $^1H-^{15}N$ steady state NOE experiment. The results revealed that HP0902 would adopt a compactly folded, all-$\beta$ topology with 11 $\beta$-strands. All of the results clearly support the notion that HP0902 belongs to the cupin superfamily of proteins.

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References

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