TY - JOUR
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
PY - 2009
Y1 - 2009
N2 - 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.
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.
UR - http://onlinelibrary.wiley.com/doi/10.1111/j.1365-2958.2009.06753.x/pdf
U2 - 10.1111/j.1365-2958.2009.06753.x
DO - 10.1111/j.1365-2958.2009.06753.x
M3 - Article
SN - 0950-382X
VL - 73
SP - 20
EP - 31
JO - Molecular Microbiology
JF - Molecular Microbiology
IS - 1
ER -