Backbone ¹H, ∨15N, and ∨13C resonance assignments and secondary-structure of the conserved hypothetical protein HP0892 of Helicobacter pylori

• Published in: Molecules and cells 2008, 25(1), , pp.138-141
• Main Authors: Han, K.D. (Seoul National University, Seoul, Republic of Korea), Park, S.J. (Seoul National University, Seoul, Republic of Korea), Jang, S.B. (Seoul National University, Seoul, Republic of Korea), Lee, B.J. (Seoul National University, Seoul, Republic of Korea), E-mail: [e-mail]
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; backbone resonance assignment; Bacterial Proteins - chemistry; Bacterial Proteins - genetics; HELICOBACTER PYLORI; Helicobacter pylori - chemistry; HP0892; hypothetical protein; Models, Molecular; Molecular Sequence Data; NMR; Nuclear Magnetic Resonance, Biomolecular; Protein Structure, Secondary; unknown protein; 생물학
• ISSN: 1016-8478; 0219-1032
• DOI: 10.1016/S1016-8478(23)17562-5

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, Cα, Cβ 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.