Open AccessHP0902 from Helicobacter pylori is a thermostable, dimeric protein belonging to an all-β topology of the cupin superfamily
Author(s) -
Dae-Won Sim,
Yoo-Sup Lee,
Ji Hun Kim,
MinDuk Seo,
Bong-Jin Lee,
HyungSik Won
Publication year - 2009
Publication title -
bmb reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.511
H-Index - 77
eISSN - 1976-670X
pISSN - 1976-6696
DOI - 10.5483/bmbrep.2009.42.6.387
Subject(s) - structural genomics , circular dichroism , dimer , heteronuclear molecule , chemistry , nuclear magnetic resonance spectroscopy , protein structure , stereochemistry , topology (electrical circuits) , protein secondary structure , crystallography , biochemistry , organic chemistry , mathematics , combinatorics
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.