Three-dimensional structure of the E. coli DMA-binding protein FIS

@article{Kostrewa1991ThreedimensionalSO,
  title={Three-dimensional structure of the E. coli DMA-binding protein FIS},
  author={D. Kostrewa and J. Granzin and C. Koch and Hui-Woog Choe and S. Raghunathan and W. Wolf and J. Labahn and R. Kahmann and W. Saenger},
  journal={Nature},
  year={1991},
  volume={349},
  pages={178-180}
}
  • D. Kostrewa, J. Granzin, +6 authors W. Saenger
  • Published 1991
  • Biology, Medicine
  • Nature
  • THE factor for inversion stimulation, FIS, is involved in several cellular processes, including site-specific recombination and tran-scriptional activation1–4. In the reactions catalysed by the DNA invertases Gin, Hin and Cin, FIS stimulates recombination by binding to an enhancer sequence1. Within the enhancer, two FIS dimers (each 2 x 98 amino acids)5–7 bind to two 15-base-pair consensus sequences8,9 (Fig. 1) and induce bending of DNA10,11. Current models propose that the enhancer–FIS complex… CONTINUE READING
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