Crystal structure of the apo-PerR-Zn protein from Bacillus subtilis

Daouda A K Traore, Abdelnasser El Ghazouani, Sougandi Ilango, Jerome Dupuy, Lilian Jacquamet, Jean-Luc Ferrer, Christelle Caux-Thang, Victor Duarte, Jean-Marc Latour

Research output: Contribution to journalArticleResearchpeer-review

Abstract

Bacteria adapt to elevated levels of Reactive Oxygen Species (ROS) by increasing the expression of defence and repair proteins, which is regulated by ROS responsive transcription factors. In Bacillus subtilis the zinc protein PerR, a peroxide sensor that binds DNA in the presence of a regulatory metal Mn2+ or Fe2+, mediates the adaptive response to 2O2. This study presents the first crystal structure of apo-PerR-Zn which shows that all four cysteine residues of the protein are involved in zinc co-ordination. The Zn(Cys)4 site locks the dimerization domain and stabilizes the dimer. Sequence alignment of PerR-like proteins supports that this structural site may constitute a distinctive feature of this class of peroxide stress regulators.
Original languageEnglish
Pages (from-to)1211 - 1219
Number of pages9
JournalMolecular Microbiology
Volume61
Issue number5
DOIs
Publication statusPublished - 2006
Externally publishedYes

Cite this

Traore, D. A. K., El Ghazouani, A., Ilango, S., Dupuy, J., Jacquamet, L., Ferrer, J-L., ... Latour, J-M. (2006). Crystal structure of the apo-PerR-Zn protein from Bacillus subtilis. Molecular Microbiology, 61(5), 1211 - 1219. https://doi.org/10.1111/j.1365-2958.2006.05313.x
Traore, Daouda A K ; El Ghazouani, Abdelnasser ; Ilango, Sougandi ; Dupuy, Jerome ; Jacquamet, Lilian ; Ferrer, Jean-Luc ; Caux-Thang, Christelle ; Duarte, Victor ; Latour, Jean-Marc. / Crystal structure of the apo-PerR-Zn protein from Bacillus subtilis. In: Molecular Microbiology. 2006 ; Vol. 61, No. 5. pp. 1211 - 1219.
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Traore, DAK, El Ghazouani, A, Ilango, S, Dupuy, J, Jacquamet, L, Ferrer, J-L, Caux-Thang, C, Duarte, V & Latour, J-M 2006, 'Crystal structure of the apo-PerR-Zn protein from Bacillus subtilis' Molecular Microbiology, vol. 61, no. 5, pp. 1211 - 1219. https://doi.org/10.1111/j.1365-2958.2006.05313.x

Crystal structure of the apo-PerR-Zn protein from Bacillus subtilis. / Traore, Daouda A K; El Ghazouani, Abdelnasser; Ilango, Sougandi; Dupuy, Jerome; Jacquamet, Lilian; Ferrer, Jean-Luc; Caux-Thang, Christelle; Duarte, Victor; Latour, Jean-Marc.

In: Molecular Microbiology, Vol. 61, No. 5, 2006, p. 1211 - 1219.

Research output: Contribution to journalArticleResearchpeer-review

TY - JOUR

T1 - Crystal structure of the apo-PerR-Zn protein from Bacillus subtilis

AU - Traore, Daouda A K

AU - El Ghazouani, Abdelnasser

AU - Ilango, Sougandi

AU - Dupuy, Jerome

AU - Jacquamet, Lilian

AU - Ferrer, Jean-Luc

AU - Caux-Thang, Christelle

AU - Duarte, Victor

AU - Latour, Jean-Marc

PY - 2006

Y1 - 2006

N2 - Bacteria adapt to elevated levels of Reactive Oxygen Species (ROS) by increasing the expression of defence and repair proteins, which is regulated by ROS responsive transcription factors. In Bacillus subtilis the zinc protein PerR, a peroxide sensor that binds DNA in the presence of a regulatory metal Mn2+ or Fe2+, mediates the adaptive response to 2O2. This study presents the first crystal structure of apo-PerR-Zn which shows that all four cysteine residues of the protein are involved in zinc co-ordination. The Zn(Cys)4 site locks the dimerization domain and stabilizes the dimer. Sequence alignment of PerR-like proteins supports that this structural site may constitute a distinctive feature of this class of peroxide stress regulators.

AB - Bacteria adapt to elevated levels of Reactive Oxygen Species (ROS) by increasing the expression of defence and repair proteins, which is regulated by ROS responsive transcription factors. In Bacillus subtilis the zinc protein PerR, a peroxide sensor that binds DNA in the presence of a regulatory metal Mn2+ or Fe2+, mediates the adaptive response to 2O2. This study presents the first crystal structure of apo-PerR-Zn which shows that all four cysteine residues of the protein are involved in zinc co-ordination. The Zn(Cys)4 site locks the dimerization domain and stabilizes the dimer. Sequence alignment of PerR-like proteins supports that this structural site may constitute a distinctive feature of this class of peroxide stress regulators.

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DO - 10.1111/j.1365-2958.2006.05313.x

M3 - Article

VL - 61

SP - 1211

EP - 1219

JO - Molecular Microbiology

JF - Molecular Microbiology

SN - 0950-382X

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