Structural characterization of the active form of PerR: insights into the metal-induced activation of PerR and Fur proteins for DNA binding-Reference-Cited by-同舟云学术

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

Published:2009-07 Issue:1 Volume:73 Page:20-31
ISSN:0950-382X
Container-title:Molecular Microbiology
language:en
Short-container-title:

Author:

Jacquamet L.,Traoré D. A. K.,Ferrer J.-L.,Proux O.,Testemale D.,Hazemann J.-L.,Nazarenko E.,El Ghazouani A.,Caux-Thang C.,Duarte V.,Latour J.-M.

Publisher

Wiley

Subject

Molecular Biology,Microbiology

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1365-2958.2009.06753.x/fullpdf

Reference44 articles.

1. Spectroscopic and saturation magnetization properties of the manganese- and cobalt-substituted Fur (ferric uptake regulation) protein from Escherichia coli;Adrait;Biochemistry,1999

2. Structural basis for the specialization of Nur, a nickel-specific Fur homolog, in metal sensing and DNA recognition;An;Nucleic Acids Res,2009

3. Zinc through the three domains of life;Andreini;J Proteome Res,2006

4. Bacillus subtilis contains multiple Fur homologues: identification of the iron uptake (Fur) and peroxide regulon (PerR) repressors;Bsat;Mol Microbiol,1998

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