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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 

Three-dimensional crystal structures of Escherichia coli met repressor with and without corepressor.

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.[1]

References

  1. Three-dimensional crystal structures of Escherichia coli met repressor with and without corepressor. Rafferty, J.B., Somers, W.S., Saint-Girons, I., Phillips, S.E. Nature (1989) [Pubmed]
 
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