Abstract
The three-dimensional crystal structure of met repressor, in the presence or absence of bound corepressor (S-adenosylmethionine), shows a dimer of intertwined monomers, which do not have the helix-turn-helix motif characteristic of other bacterial repressor and activator structures. We propose that the interaction of met repressor with DNA occurs through either a pair of symmetry-related α-helices or a pair of β-strands, and suggest a model for binding of several dimers to met operator regions.
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Rafferty, J., Somers, W., Saint-Girons, I. et al. Three-dimensional crystal structures of Escherichia coli met repressor with and without corepressor. Nature 341, 705–710 (1989). https://doi.org/10.1038/341705a0
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DOI: https://doi.org/10.1038/341705a0
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