Abstract
The haem-binding protein HbpS from Streptomyces reticuli was crystallized and diffraction data were collected to a maximal resolution of 2.25 Å. Streptomyces reticuli is a soil-growing Gram-positive bacteria that has been shown to secrete a novel haem-binding protein known as HbpS. Sequence analysis reveals that homologues of HbpS are found in a wide variety of bacteria, including different Actinobacteria and the Gram-negative Vibrio cholera and Klebsiella pneumoniae. The in vivo production of HbpS is greatly increased when S. reticuli is cultured in the presence of the natural antibiotic haemin (Fe{sup 3+} oxidized form of haem). Mutational analysis demonstrated that HbpS significantly increases the resistance of S. reticuli to toxic concentrations of haemin. Previous data show that the presence of the newly identified two-component sensor system SenS–SenR also considerably enhances the resistance of S. reticuli to haemin and the redox-cycling compound plumbagin, suggesting a role in the sensing of redox changes. Specific interaction between HbpS and SenS–SenR, which regulates the expression of the catalase–peroxidase CpeB, as well as HbpS, has been demonstrated in vitro. HbpS has been recombinantly overexpressed, purified and crystallized in space group P2{sub 1}3, with a cell edge of 152.5 Å. Diffraction data were recorded to a maximal
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Zou, Peijian;
[1]
Institute of Structural Biology, Helmholtz Zentrum München, Ingolstädter Landstrasse 1, 85764 Neuherberg (Germany)];
Groves, Matthew R.;
[1]
Viale-Bouroncle, Sandra D.;
Ortiz de Orué Lucana, Darío, E-mail: ortiz@biologie.uni-osnabrueck.de [Universität Osnabrück, FB Biologie/Chemie, Angewandte Genetik der Mikroorganismen, Barbarastrasse 13, 49069 Osnabrück (Germany);
EMBL Outstation Hamburg, c/o DESY, Notkestrasse 85, 22607 Hamburg (Germany)]
- EMBL Outstation Hamburg, c/o DESY, Notkestrasse 85, 22607 Hamburg (Germany)
Citation Formats
Zou, Peijian, Institute of Structural Biology, Helmholtz Zentrum München, Ingolstädter Landstrasse 1, 85764 Neuherberg (Germany)], Groves, Matthew R., Viale-Bouroncle, Sandra D., Ortiz de Orué Lucana, Darío, E-mail: ortiz@biologie.uni-osnabrueck.de [Universität Osnabrück, FB Biologie/Chemie, Angewandte Genetik der Mikroorganismen, Barbarastrasse 13, 49069 Osnabrück (Germany), and EMBL Outstation Hamburg, c/o DESY, Notkestrasse 85, 22607 Hamburg (Germany)].
Crystallization and preliminary characterization of a novel haem-binding protein of Streptomyces reticuli.
United Kingdom: N. p.,
2008.
Web.
doi:10.1107/S1744309108008348.
Zou, Peijian, Institute of Structural Biology, Helmholtz Zentrum München, Ingolstädter Landstrasse 1, 85764 Neuherberg (Germany)], Groves, Matthew R., Viale-Bouroncle, Sandra D., Ortiz de Orué Lucana, Darío, E-mail: ortiz@biologie.uni-osnabrueck.de [Universität Osnabrück, FB Biologie/Chemie, Angewandte Genetik der Mikroorganismen, Barbarastrasse 13, 49069 Osnabrück (Germany), & EMBL Outstation Hamburg, c/o DESY, Notkestrasse 85, 22607 Hamburg (Germany)].
Crystallization and preliminary characterization of a novel haem-binding protein of Streptomyces reticuli.
United Kingdom.
https://doi.org/10.1107/S1744309108008348
Zou, Peijian, Institute of Structural Biology, Helmholtz Zentrum München, Ingolstädter Landstrasse 1, 85764 Neuherberg (Germany)], Groves, Matthew R., Viale-Bouroncle, Sandra D., Ortiz de Orué Lucana, Darío, E-mail: ortiz@biologie.uni-osnabrueck.de [Universität Osnabrück, FB Biologie/Chemie, Angewandte Genetik der Mikroorganismen, Barbarastrasse 13, 49069 Osnabrück (Germany), and EMBL Outstation Hamburg, c/o DESY, Notkestrasse 85, 22607 Hamburg (Germany)].
2008.
"Crystallization and preliminary characterization of a novel haem-binding protein of Streptomyces reticuli."
United Kingdom.
https://doi.org/10.1107/S1744309108008348.
@misc{etde_22360569,
title = {Crystallization and preliminary characterization of a novel haem-binding protein of Streptomyces reticuli}
author = {Zou, Peijian, Institute of Structural Biology, Helmholtz Zentrum München, Ingolstädter Landstrasse 1, 85764 Neuherberg (Germany)], Groves, Matthew R., Viale-Bouroncle, Sandra D., Ortiz de Orué Lucana, Darío, E-mail: ortiz@biologie.uni-osnabrueck.de [Universität Osnabrück, FB Biologie/Chemie, Angewandte Genetik der Mikroorganismen, Barbarastrasse 13, 49069 Osnabrück (Germany), and EMBL Outstation Hamburg, c/o DESY, Notkestrasse 85, 22607 Hamburg (Germany)]}
abstractNote = {The haem-binding protein HbpS from Streptomyces reticuli was crystallized and diffraction data were collected to a maximal resolution of 2.25 Å. Streptomyces reticuli is a soil-growing Gram-positive bacteria that has been shown to secrete a novel haem-binding protein known as HbpS. Sequence analysis reveals that homologues of HbpS are found in a wide variety of bacteria, including different Actinobacteria and the Gram-negative Vibrio cholera and Klebsiella pneumoniae. The in vivo production of HbpS is greatly increased when S. reticuli is cultured in the presence of the natural antibiotic haemin (Fe{sup 3+} oxidized form of haem). Mutational analysis demonstrated that HbpS significantly increases the resistance of S. reticuli to toxic concentrations of haemin. Previous data show that the presence of the newly identified two-component sensor system SenS–SenR also considerably enhances the resistance of S. reticuli to haemin and the redox-cycling compound plumbagin, suggesting a role in the sensing of redox changes. Specific interaction between HbpS and SenS–SenR, which regulates the expression of the catalase–peroxidase CpeB, as well as HbpS, has been demonstrated in vitro. HbpS has been recombinantly overexpressed, purified and crystallized in space group P2{sub 1}3, with a cell edge of 152.5 Å. Diffraction data were recorded to a maximal resolution of 2.25 Å and phases were obtained using the SAD method from crystals briefly soaked in high concentrations of sodium bromide.}
doi = {10.1107/S1744309108008348}
journal = []
issue = {Pt 5}
volume = {64}
journal type = {AC}
place = {United Kingdom}
year = {2008}
month = {May}
}
title = {Crystallization and preliminary characterization of a novel haem-binding protein of Streptomyces reticuli}
author = {Zou, Peijian, Institute of Structural Biology, Helmholtz Zentrum München, Ingolstädter Landstrasse 1, 85764 Neuherberg (Germany)], Groves, Matthew R., Viale-Bouroncle, Sandra D., Ortiz de Orué Lucana, Darío, E-mail: ortiz@biologie.uni-osnabrueck.de [Universität Osnabrück, FB Biologie/Chemie, Angewandte Genetik der Mikroorganismen, Barbarastrasse 13, 49069 Osnabrück (Germany), and EMBL Outstation Hamburg, c/o DESY, Notkestrasse 85, 22607 Hamburg (Germany)]}
abstractNote = {The haem-binding protein HbpS from Streptomyces reticuli was crystallized and diffraction data were collected to a maximal resolution of 2.25 Å. Streptomyces reticuli is a soil-growing Gram-positive bacteria that has been shown to secrete a novel haem-binding protein known as HbpS. Sequence analysis reveals that homologues of HbpS are found in a wide variety of bacteria, including different Actinobacteria and the Gram-negative Vibrio cholera and Klebsiella pneumoniae. The in vivo production of HbpS is greatly increased when S. reticuli is cultured in the presence of the natural antibiotic haemin (Fe{sup 3+} oxidized form of haem). Mutational analysis demonstrated that HbpS significantly increases the resistance of S. reticuli to toxic concentrations of haemin. Previous data show that the presence of the newly identified two-component sensor system SenS–SenR also considerably enhances the resistance of S. reticuli to haemin and the redox-cycling compound plumbagin, suggesting a role in the sensing of redox changes. Specific interaction between HbpS and SenS–SenR, which regulates the expression of the catalase–peroxidase CpeB, as well as HbpS, has been demonstrated in vitro. HbpS has been recombinantly overexpressed, purified and crystallized in space group P2{sub 1}3, with a cell edge of 152.5 Å. Diffraction data were recorded to a maximal resolution of 2.25 Å and phases were obtained using the SAD method from crystals briefly soaked in high concentrations of sodium bromide.}
doi = {10.1107/S1744309108008348}
journal = []
issue = {Pt 5}
volume = {64}
journal type = {AC}
place = {United Kingdom}
year = {2008}
month = {May}
}