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

doi:10.1074/jbc.M113.456590

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 journal › Article › peer-review

50 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 language	English (US)
Pages (from-to)	18311-18324
Number of pages	14
Journal	Journal of Biological Chemistry
Volume	288
Issue number	25
DOIs	https://doi.org/10.1074/jbc.M113.456590
State	Published - Jun 21 2013

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

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

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.",

author = "Nishanth Makthal and Sheila Rastegari and Misu Sanson and Zhen Ma and Olsen, \{Randall J.\} and Helmann, \{John D.\} and Musser, \{James M.\} and Muthiah Kumaraswami",

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T1 - Crystal structure of peroxide stress regulator from streptococcus pyogenes provides functional insights into the mechanism of oxidative stress sensing

AU - Makthal, Nishanth

AU - Rastegari, Sheila

AU - Sanson, Misu

AU - Ma, Zhen

AU - Olsen, Randall J.

AU - Helmann, John D.

AU - Musser, James M.

AU - Kumaraswami, Muthiah

PY - 2013/6/21

Y1 - 2013/6/21

N2 - 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.

AB - 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.

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U2 - 10.1074/jbc.M113.456590

DO - 10.1074/jbc.M113.456590

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SP - 18311

EP - 18324

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 25

ER -

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

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