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

@article{Rafferty1989ThreedimensionalCS,
  title={Three-dimensional crystal structures of Escherichia coli met repressor with and without corepressor},
  author={John B. Rafferty and William S. Somers and Isabella Saint-Girons and Simon E V Phillips},
  journal={Nature},
  year={1989},
  volume={341},
  pages={705-710}
}
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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