Backbone 1H, 15N, and 13C Resonance Assignments and Secondary-Structure of Conserved Hypothetical Protein HP0894 from Helicobacter pylori

  • Han, Kyung-Doo (National Laboratory of Membrane Protein Structure (MPS), Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University) ;
  • Park, Sung-Jean (National Laboratory of Membrane Protein Structure (MPS), Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University) ;
  • Lee, Bong-Jin (National Laboratory of Membrane Protein Structure (MPS), Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University)
  • Received : 2005.09.23
  • Accepted : 2005.09.30
  • Published : 2005.12.31


HP0894 (SwissProt/TrEMBL ID O25554) is an 88-residue conserved hypothetical protein from Helicobacter pylori strain 26695 with a calculated pI of 8.5 and a molecular weight of 10.38 kDa. Proteins with sequence similarity to HP0894 exist in Vibrio choierae, Enterococcus faecalis, Campylobacter jejuni, Streptococcus pneumoniae, Haemophilus influenzae, Escherichia coli O157, etc. Here we report the sequence-specific backbone resonance assignments of HP0894. About 97.5% (418/429) of the HN, N, CO, $C{\alpha}$, $C{\beta}$ resonances of the 88 residues of HP0894 were assigned. On the basis of these 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 HP0894, and studying its interaction with its substrates, if any, and/or with other proteins.


Backbone Resonance Assignment;Helicobacter pylori;HP0894;Hypothetical Protein;NMR;Unknown Protein


Supported by : Ministry of Health & Welfare


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