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J. Biol. Chem., Vol. 276, Issue 23, 20641-20647, June 8, 2001

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Oxyanion Binding Alters Conformation and Quaternary Structure of the C-terminal Domain of the Transcriptional Regulator ModE
IMPLICATIONS FOR MOLYBDATE-DEPENDENT REGULATION, SIGNALING, STORAGE, AND TRANSPORT^*

David G. Gourley^§, Alexander W. Schüttelkopf^§, Lisa A. Anderson, Nicholas C. Price^¶, David H. Boxer, and William N. Hunter^**

From  The Wellcome Trust Biocentre, University of Dundee, Dundee, DD1 5EH and the ^¶ Department of Biological Sciences, University of Stirling, Stirling, FK9 4LA, United Kingdom

The molybdate-dependent transcriptional regulator ModE of Escherichia coli functions as a sensor of intracellular molybdate concentration and a regulator for the transcription of several operons that control the uptake and utilization of molybdenum. We present two high-resolution crystal structures of the C-terminal oxyanion-binding domain in complex with molybdate and tungstate. The ligands bind between subunits at the dimerization interface, and analysis reveals that oxyanion selectivity is determined primarily by size. The relevance of the structures is indicated by fluorescence measurements, which show that the oxyanion binding properties of the C-terminal domain of ModE are similar to those of the full-length protein. Comparisons with the apoprotein structure have identified structural rearrangements that occur on binding oxyanion. This molybdate-dependent conformational switch promotes a change in shape and alterations to the surface of the protein and may provide the signal for recruitment of other proteins to construct the machinery for transcription. Sequence and structure-based comparisons lead to a classification of molybdate-binding proteins.

The atomic coordinates and the structure factors (code 1H9R/1H9S) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

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