Abstract
Background: PerR from Streptococcus pyogenes is critical for bacterial virulence. Results: We determined the crystal structure of PerR and deduced the molecular mechanism of stress sensing and gene regulation by PerR. Conclusion: A novel structural motif present at theNterminus of PerR is important for metal binding, oxidative stress sensing, and GAS virulence. Significance: The structural elements of PerR identified here could potentially be targeted for therapeutic development.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 18311-18324 |
| Number of pages | 14 |
| Journal | Journal of Biological Chemistry |
| Volume | 288 |
| Issue number | 25 |
| DOIs | |
| State | Published - Jun 21 2013 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology