1x93
NMR Structure of Helicobacter pylori HP0222
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| Gene: | HP0222 (Helicobacter pylori 26695) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
OverviewOverview
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.
About this StructureAbout this Structure
1X93 is a Single protein structure of sequence from Helicobacter pylori 26695. Full crystallographic information is available from OCA.
ReferenceReference
Helicobacter pylori protein HP0222 belongs to Arc/MetJ family of transcriptional regulators., Popescu A, Karpay A, Israel DA, Peek RM Jr, Krezel AM, Proteins. 2005 May 1;59(2):303-11. PMID:15723352
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