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Title: Three-dimensional crystal structures of Escherichia coli met repressor with and without corepressor. Author: Rafferty JB, Somers WS, Saint-Girons I, Phillips SE. Journal: Nature; 1989 Oct 26; 341(6244):705-10. PubMed ID: 2677753. 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.[Abstract] [Full Text] [Related] [New Search]