1X93
NMR Structure of Helicobacter pylori HP0222
Summary for 1X93
| Entry DOI | 10.2210/pdb1x93/pdb |
| Descriptor | hypothetical protein HP0222 (1 entity in total) |
| Functional Keywords | hp0222, jhp0208, helicobacter, pylori, transcription, regulator, arc, metj, mnt, parg, copg, repa |
| Biological source | Helicobacter pylori |
| Total number of polymer chains | 2 |
| Total formula weight | 13142.80 |
| Authors | Popescu, A.,Karpay, A.,Israel, D.,Peek Jr., R.M.,Krezel, A.M. (deposition date: 2004-08-19, release date: 2005-03-22, Last modification date: 2024-05-01) |
| Primary citation | Popescu, A.,Karpay, A.,Israel, D.A.,Peek Jr., R.M.,Krezel, A.M. Helicobacter pylori protein HP0222 belongs to Arc/MetJ family of transcriptional regulators. Proteins, 59:303-311, 2005 Cited by PubMed Abstract: Helicobacter pylori is a widespread human bacterial pathogen responsible for inducing gastric and duodenal ulcers and gastric cancers. To date, only 16 protein structures from this organism have been determined, and more than 30% of its 1500 protein functions remain unknown. We report the biochemical characterization, the tertiary structure determined by solution nuclear magnetic resonance (NMR) methods and the putative function of the previously uncharacterized protein HP0222 (JHP0208) from H. pylori. Recombinant HP0222 behaves as a dimer in crosslinking and size exclusion chromatography experiments. The structure consists of a ribbon-helix-helix fold characteristic of transcription factors of the Arc/MetJ family, which all bind DNA as higher order oligomers. Electrophoretic mobility shift assays reveal that HP0222 binds to double-stranded DNA. Previous studies have shown significant increases in transcription levels of HP0222 in response to acid shock and adherence to gastric epithelial cells. To assess possible involvement of HP0222 in acid resistance, we constructed and assayed an H. pylori HP0222 null mutant. We propose that HP0222 is a novel transcriptional regulator in H. pylori. PubMed: 15723352DOI: 10.1002/prot.20406 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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