Three-dimensional crystal structures of Escherichia coli met repressor with and without corepressor |
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Authors: | J B Rafferty W S Somers I Saint-Girons S E Phillips |
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Affiliation: | Astbury Department of Biophysics, University of Leeds, UK. |
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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 alpha-helices or a pair of beta-strands, and suggest a model for binding of several dimers to met operator regions. |
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