HP0902 from Helicobacter pylori is a thermostable, dimeric protein belonging to an all-beta topology of the cupin superfamily.
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 degrees 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 (1)H-(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.
Sim
Dae-Won
DW
Department of Biotechnology, College of Biomedical and Health Science, Konkuk University, Chungju, 380-701, Korea.
Lee
Yoo-Sup
YS
Kim
Ji-Hun
JH
Seo
Min-Duk
MD
Lee
Bong-Jin
BJ
Won
Hyung-Sik
HS
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism / Q000502:physiology*; D016480:Helicobacter pylori / Q000378:metabolism; D008969:Molecular Sequence Data; D005810:Multigene Family; D017510:Protein Folding; D055503:Protein Multimerization; D055550:Protein Stability; D017433:Protein Structure, Secondary; D013696:Temperature
D001426:Bacterial Proteins