Download MendeleyThe high-resolution crystal structure of the molybdate-dependent transcriptional regulator (ModE) from Escherichia coli: a novel combination of domain folds.
Hall, D.R., Gourley, D.G., Leonard, G.A., Duke, E.M., Anderson, L.A., Boxer, D.H., Hunter, W.N.(1999) EMBO J 18: 1435-1436
- PubMed: 10075916
- DOI: https://doi.org/10.1093/emboj/18.6.1435
- Primary Citation of Related Structures:
1B9M, 1B9N - PubMed Abstract:
The molybdate-dependent transcriptional regulator (ModE) from Escherichia coli functions as a sensor of molybdate concentration and a regulator for transcription of operons involved in the uptake and utilization of the essential element, molybdenum. We have determined the structure of ModE using multi-wavelength anomalous dispersion. Selenomethionyl and native ModE models are refined to 1. 75 and 2.1 A, respectively and describe the architecture and structural detail of a complete transcriptional regulator. ModE is a homodimer and each subunit comprises N- and C-terminal domains. The N-terminal domain carries a winged helix-turn-helix motif for binding to DNA and is primarily responsible for ModE dimerization. The C-terminal domain contains the molybdate-binding site and residues implicated in binding the oxyanion are identified. This domain is divided into sub-domains a and b which have similar folds, although the organization of secondary structure elements varies. The sub-domain fold is related to the oligomer binding-fold and similar to that of the subunits of several toxins which are involved in extensive protein-protein interactions. This suggests a role for the C-terminal domain in the formation of the ModE-protein-DNA complexes necessary to regulate transcription. Modelling of ModE interacting with DNA suggests that a large distortion of DNA is not necessary for complex formation.
Organizational Affiliation:
The Wellcome Trust Building, Department of Biochemistry, University of Dundee, Dundee DD1 5EH, UK.
