Structural characterization of the active form of PerR: Insights into the metal-induced activation of PerR and fur proteins for DNA binding

Lilian Jacquamet, Daouda A K Traore, Jean -Luc Ferrer, O Proux, Denis Testemale, Jean -Louis Hazemann, E Nazarenko, Abdelnasser El Ghazouani, Christelle Caux-Thang, Victor Duarte, Jean -Marc Latour

Research output: Contribution to journalArticleResearchpeer-review

Abstract

In Bacillus subtilis, the transcription factor PerR is an iron dependant sensor of H2O2. The sensing mechanism relies on a selective metal catalysed oxidation of two histidine residues of the regulatory site. Here we present the first crystal structure of the active PerR protein in complex with a Mn2+ ion. In addition, X-ray absorption spectroscopy experiments were performed to characterize the corresponding iron form of the protein. Both studies reveal a penta- coordinate arrangement of the regulatory site that involves three histidines and two aspartates. One of the histidine ligand belongs to the N-terminal domain. Binding of this residue to the regulatory metal allows the protein to adopt a caliper-like conformation suited to DNA binding. Since this histidine is conserved in all PerR and a vast majority of Fur proteins, it is likely that the allosteric switch induced by the regulatory metal is general for this family of metalloregulators.
Original languageEnglish
Pages (from-to)20 - 31
Number of pages12
JournalMolecular Microbiology
Volume73
Issue number1
DOIs
Publication statusPublished - 2009
Externally publishedYes

Cite this

Jacquamet, Lilian ; Traore, Daouda A K ; Ferrer, Jean -Luc ; Proux, O ; Testemale, Denis ; Hazemann, Jean -Louis ; Nazarenko, E ; El Ghazouani, Abdelnasser ; Caux-Thang, Christelle ; Duarte, Victor ; Latour, Jean -Marc. / Structural characterization of the active form of PerR: Insights into the metal-induced activation of PerR and fur proteins for DNA binding. In: Molecular Microbiology. 2009 ; Vol. 73, No. 1. pp. 20 - 31.
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abstract = "In Bacillus subtilis, the transcription factor PerR is an iron dependant sensor of H2O2. The sensing mechanism relies on a selective metal catalysed oxidation of two histidine residues of the regulatory site. Here we present the first crystal structure of the active PerR protein in complex with a Mn2+ ion. In addition, X-ray absorption spectroscopy experiments were performed to characterize the corresponding iron form of the protein. Both studies reveal a penta- coordinate arrangement of the regulatory site that involves three histidines and two aspartates. One of the histidine ligand belongs to the N-terminal domain. Binding of this residue to the regulatory metal allows the protein to adopt a caliper-like conformation suited to DNA binding. Since this histidine is conserved in all PerR and a vast majority of Fur proteins, it is likely that the allosteric switch induced by the regulatory metal is general for this family of metalloregulators.",
author = "Lilian Jacquamet and Traore, {Daouda A K} and Ferrer, {Jean -Luc} and O Proux and Denis Testemale and Hazemann, {Jean -Louis} and E Nazarenko and {El Ghazouani}, Abdelnasser and Christelle Caux-Thang and Victor Duarte and Latour, {Jean -Marc}",
year = "2009",
doi = "10.1111/j.1365-2958.2009.06753.x",
language = "English",
volume = "73",
pages = "20 -- 31",
journal = "Molecular Microbiology",
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Jacquamet, L, Traore, DAK, Ferrer, J-L, Proux, O, Testemale, D, Hazemann, J-L, Nazarenko, E, El Ghazouani, A, Caux-Thang, C, Duarte, V & Latour, J-M 2009, 'Structural characterization of the active form of PerR: Insights into the metal-induced activation of PerR and fur proteins for DNA binding' Molecular Microbiology, vol. 73, no. 1, pp. 20 - 31. https://doi.org/10.1111/j.1365-2958.2009.06753.x

Structural characterization of the active form of PerR: Insights into the metal-induced activation of PerR and fur proteins for DNA binding. / Jacquamet, Lilian; Traore, Daouda A K; Ferrer, Jean -Luc; Proux, O; Testemale, Denis; Hazemann, Jean -Louis; Nazarenko, E; El Ghazouani, Abdelnasser; Caux-Thang, Christelle; Duarte, Victor; Latour, Jean -Marc.

In: Molecular Microbiology, Vol. 73, No. 1, 2009, p. 20 - 31.

Research output: Contribution to journalArticleResearchpeer-review

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T1 - Structural characterization of the active form of PerR: Insights into the metal-induced activation of PerR and fur proteins for DNA binding

AU - Jacquamet, Lilian

AU - Traore, Daouda A K

AU - Ferrer, Jean -Luc

AU - Proux, O

AU - Testemale, Denis

AU - Hazemann, Jean -Louis

AU - Nazarenko, E

AU - El Ghazouani, Abdelnasser

AU - Caux-Thang, Christelle

AU - Duarte, Victor

AU - Latour, Jean -Marc

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AB - In Bacillus subtilis, the transcription factor PerR is an iron dependant sensor of H2O2. The sensing mechanism relies on a selective metal catalysed oxidation of two histidine residues of the regulatory site. Here we present the first crystal structure of the active PerR protein in complex with a Mn2+ ion. In addition, X-ray absorption spectroscopy experiments were performed to characterize the corresponding iron form of the protein. Both studies reveal a penta- coordinate arrangement of the regulatory site that involves three histidines and two aspartates. One of the histidine ligand belongs to the N-terminal domain. Binding of this residue to the regulatory metal allows the protein to adopt a caliper-like conformation suited to DNA binding. Since this histidine is conserved in all PerR and a vast majority of Fur proteins, it is likely that the allosteric switch induced by the regulatory metal is general for this family of metalloregulators.

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