Structural analysis of the DNA-binding domain of the Helicobacter pylori response regulator ArsR

Shobhana S. Gupta, Brendan N. Borin, Timothy L. Cover, Andrzej M. Krezel

Research output: Contribution to journalArticlepeer-review

11 Scopus citations


The Helicobacter pylori ArsS-ArsR two-component signal transduction system, comprised of a sensor histidine kinase (ArsS) and a response regulator (ArsR), allows the bacteria to regulate gene expression in response to acidic pH. We expressed and purified the full-length ArsR protein and the DNA-binding domain of ArsR (ArsR-DBD), and we analyzed the tertiary structure of the ArsR-DBD using solution nuclear magnetic resonance (NMR) methods. Both the full-length ArsR and the ArsR-DBD behaved as monomers in size exclusion chromatography experiments. The structure of ArsR-DBD consists of an N-terminal four-stranded β-sheet, a helical core, and a C-terminal β-hairpin. The overall tertiary fold of the Ars-RDBD is most closely related to DBD structures of the OmpR/PhoB subfamily of bacterial response regulators. However, the orientation of the N-terminal β-sheet with respect to the rest of the DNA-binding domain is substantially different in ArsR compared with the orientation in related response regulators. Molecular modeling of an ArsR-DBD-DNA complex permits identification of protein elements that are predicted to bind target DNA sequences and thereby regulate gene transcription in H. pylori.

Original languageEnglish
Pages (from-to)6536-6545
Number of pages10
JournalJournal of Biological Chemistry
Issue number10
StatePublished - Mar 6 2009


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