1h9r: Difference between revisions

Revision as of 17:27, 5 November 2007

TUNGSTATE BOUND COMPLEX DIMOP DOMAIN OF MODE FROM E.COLI

OverviewOverview

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.

About this StructureAbout this Structure

1H9R is a Single protein structure of sequence from Escherichia coli with WO4 and NI as ligands. Structure known Active Sites: AC1, AC2 and AC3. Full crystallographic information is available from OCA.

ReferenceReference

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., Gourley DG, Schuttelkopf AW, Anderson LA, Price NC, Boxer DH, Hunter WN, J Biol Chem. 2001 Jun 8;276(23):20641-7. Epub 2001 Mar 20. PMID:11259434

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	[[Category: transcription regulator]]		[[Category: transcription regulator]]

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