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Architecture of a protein central to iron homeostasis: crystal structure and spectroscopic analysis of the ferric uptake regulator
Author(s) -
Pohl Ehmke,
Haller Jon C.,
Mijovilovich Ana,
MeyerKlaucke Wolfram,
Garman Elspeth,
Vasil Michael L.
Publication year - 2003
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1046/j.1365-2958.2003.03337.x
Subject(s) - biology , regulator , ferric , iron homeostasis , pseudomonas aeruginosa , intracellular , bacteria , biochemistry , biophysics , zinc , siderophore , microbiology and biotechnology , chemistry , genetics , inorganic chemistry , metabolism , gene , organic chemistry
Summary Iron is an essential element for almost all organisms, although an overload of this element results in toxicity because of the formation of hydroxyl radicals. Consequently, most living entities have developed sophisticated mechanisms to control their intracellular iron concentration. In many bacteria, including the opportunistic pathogen Pseudomonas aeruginosa , this task is performed by the ferric uptake regulator (Fur). Fur controls a wide variety of basic physiological processes including iron uptake systems and the expression of exotoxin A. Here, we present the first crystal structure of Fur from P. aeruginosa in complex with Zn 2+ determined at a resolution of 1.8 Å. Furthermore, X‐ray absorption spectroscopic measurements and microPIXE analysis were performed in order to characterize the distinct zinc and iron binding sites in solution. The combination of these complementary techniques enables us to present a model for the activation and DNA binding of the Fur protein.