• BMB Reports
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• v.42 no.6
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• pp.387-392
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• 2009

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.

• Journal of the Korean Magnetic Resonance Society
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• v.21 no.2
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• pp.50-54
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• 2017

Cupin-superfamily proteins represent the most functionally diverse groups of proteins and include a huge number of functionally uncharacterized proteins. Recently, YaiE, a cupin protein from Escherichia coli has been suggested to be involved in a novel activity of pyrimidine/purine nucleoside phosphorylase (PPNP). In the present study, we achieved a complete backbone NMR assignments of YaiE, by a series of heteronuclear multidimensional NMR experiments on its [$^{13}C/^{15}N$]-enriched sample. Subsequently, secondary structure analysis using the assigned chemical shift values identified 10 obvious ${\beta}-strands$ and a tentative $3_{10}-helix$. Taken all together, the results constitute the first structural characterization of a putative PPNP cupin protein.