Reference : The structure of the Helicobacter pylori ferric uptake regulator Fur reveals three fu...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/10993/26360
The structure of the Helicobacter pylori ferric uptake regulator Fur reveals three functional metal binding sites.
English
Dian, Cyril [European Synchrotron Radiat Facil > Struct Biol Grp]
Vitale, Sylvia [Grenoble University > UMR 5249, Lab Chim & Biol Metaux]
Leonard, Gordon A. [European Synchrotron Radiat Facil > Struct Biol Grp]
Bahlawane, Christelle mailto [Univ Grenoble 1 > UMR 5249, Lab Chim & Biol Metaux > > ; Hannover Med School > Inst Med Microbiol > > ; Hannover Medecine School > Hosp Epidemiol]
Fauquant, Caroline [Univ Grenoble 1 > UMR 5249, Lab Chim & Biol Metaux]
Leduc, Damien [Institut Pasteur (paris) > Unite Pathogenese Helicobacter]
Muller, Cecile [Institut pasteur (paris) > Unite Pathogenese Helicobacter]
de Reuse, Hilde [Institut pasteur (Paris) > Unite Pathogenese Helicobacter]
Michaud-Soret, Isabelle [Univ Grenoble 1 > UMR 5249, Lab Chim & Biol Metaux]
Terradot, Laurent [Univ grenoble 1 > UMR 5249, Lab Chim & Biol Metaux > > ; Univ Lyon, Inst Biol & Chim Prot > UMR 5086,IFR128]
2011
Molecular microbiology
79
5
1260-75
Yes (verified by ORBilu)
International
0950-382X
1365-2958
England
[en] Amino Acid Sequence ; Bacterial Proteins/chemistry/genetics/metabolism ; Binding Sites ; DNA, Bacterial/metabolism ; Helicobacter pylori/chemistry/genetics/metabolism ; Iron/metabolism ; Molecular Sequence Data ; Protein Structure, Secondary ; Repressor Proteins/chemistry/genetics/metabolism ; Sequence Alignment
[en] Fur, the ferric uptake regulator, is a transcription factor that controls iron metabolism in bacteria. Binding of ferrous iron to Fur triggers a conformational change that activates the protein for binding to specific DNA sequences named Fur boxes. In Helicobacter pylori, HpFur is involved in acid response and is important for gastric colonization in model animals. Here we present the crystal structure of a functionally active HpFur mutant (HpFur2M; C78S-C150S) bound to zinc. Although its fold is similar to that of other Fur and Fur-like proteins, the crystal structure of HpFur reveals a unique structured N-terminal extension and an unusual C-terminal helix. The structure also shows three metal binding sites: S1 the structural ZnS(4) site previously characterized biochemically in HpFur and the two zinc sites identified in other Fur proteins. Site-directed mutagenesis and spectroscopy analyses of purified wild-type HpFur and various mutants show that the two metal binding sites common to other Fur proteins can be also metallated by cobalt. DNA protection and circular dichroism experiments demonstrate that, while these two sites influence the affinity of HpFur for DNA, only one is absolutely required for DNA binding and could be responsible for the conformational changes of Fur upon metal binding while the other is a secondary site.
http://hdl.handle.net/10993/26360
10.1111/j.1365-2958.2010.07517.x
(c) 2011 Blackwell Publishing Ltd.

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