Crystal structure of peroxide stress regulator from streptococcus pyogenes provides functional insights into the mechanism of oxidative stress sensing

Nishanth Makthal, Sheila Rastegari, Misu Sanson, Zhen Ma, Randall J. Olsen, John D. Helmann, James M. Musser, Muthiah Kumaraswami

Research output: Contribution to journalArticle

38 Scopus citations

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 languageEnglish (US)
Pages (from-to)18311-18324
Number of pages14
JournalJournal of Biological Chemistry
Volume288
Issue number25
DOIs
StatePublished - Jun 21 2013

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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