KMID : 0624620090420060387
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BMB Reports 2009 Volume.42 No. 6 p.387 ~ p.392
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HP0902 from Helicobacter pylori is a thermostable, dimeric protein belonging to an all-¥â topology of the cupin superfamily
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Sim Dae-Won
Lee Yoo-Sup Kim Ji-Hun Seo Min-Duk Lee Bong-Jin Won Hyung-Sik
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Abstract
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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 ¥â-structure and the protein was highly thermostable with a denaturing temperature higher than 70oC. Finally, the backbone NMR assignments were obtained on the [13C,15N]HP0902 and the secondary structure was determined using the chemical shift data. Additionally, the local flexibility was assessed via a heteronuclear 1H-15N steady state NOE experiment. The results revealed that HP0902 would adopt a compactly folded, all-¥â topology with 11 ¥â-strands. All of the results clearly support the notion that HP0902 belongs to the cupin superfamily of proteins.
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KEYWORD
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All-¥â topology, Cupin superfamily, Helicobacter pylori, HP0902, NMR spectroscopy, Secondary structure
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