Backbone 1H, 15N, and 13C Resonance Assignments and Secondary-Structure of the Conserved Hypothetical Protein HP0892 of Helicobacter pylori

  • Han, Kyung-Doo (Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University) ;
  • Park, Sung-Jean (Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University) ;
  • Jang, Sun-Bok (Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University) ;
  • Lee, Bong-Jin (Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University)
  • Received : 2007.07.05
  • Accepted : 2007.09.04
  • Published : 2008.02.29

Abstract

HP0892 (SwissProt/TrEMBL ID O25552) is a 90-residue conserved hypothetical protein from Helicobacter pylori strain 26695, with a calculated pI of 9.38 and a molecular mass of 10.41 kDa. It belongs to the Plasmid stabilization system protein family (PF05016) in the Pfam database. Proteins with sequence similarity to HP0892 exist in Vibrio choierae, Enterococcus faecalis, Campylobacter jejuni, Streptococcus pneumoniae, Haemophilus influenzae, Escherichia coli O157. Here we report the sequence-specific backbone resonance assignments of HP0892 using multidimentional heteronuclear NMR spectroscopy. About 97.0% (422/435) of the HN, N, CO, $C{\beta}$, $C{\alpha}$ resonances of 90 residues of HP0892 were assigned. On the basis of the resonance assignments, three helical regions and four strand regions were identified using the CSI program. This study is a prerequisite for calculating the solution structure of HP0892, and will be useful for studying its interaction with other molecules.

Keywords

References

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