1H9R

Tungstate bound complex Dimop domain of ModE from E.coli

Summary for 1H9R

• Entry DOI: 10.2210/pdb1h9r/pdb
• Related: 1B9M 1B9N 1H9S
• Descriptor: MOLYBDENUM TRANSPORT PROTEIN MODE, TUNGSTATE(VI)ION, NICKEL (II) ION, ... (4 entities in total)
• Functional Keywords: transcription regulator
• Biological source: ESCHERICHIA COLI
• Cellular location: Cytoplasm: P46930
• Total number of polymer chains: 2
• Total formula weight: 30652.17

Authors

Gourley, D.G.,Hunter, W.N. (deposition date: 2001-03-19, release date: 2001-06-19, Last modification date: 2023-12-13)

Primary citation

Gourley, D.G.,Schuttelkopf, A.W.,Anderson, L.A.,Price, N.C.,Boxer, D.H.,Hunter, W.N.
Oxyanion Binding Alters Conformational and Quaternary Structure of the C-Terminal Domain of the Transcriptional Regulator Mode; Implications for Molybdate-Dependant Regulation, Signalling, Storage and Transport
J.Biol.Chem., 276:20641-, 2001

PubMed Abstract: 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.

PubMed: 11259434
DOI: 10.1074/JBC.M100919200

Experimental method

X-RAY DIFFRACTION (1.9 Å)