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

  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},
  • 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
    138 Citations

    Topics from this paper

    Identification of the λ integrase surface that interacts with Xis reveals a residue that is also critical for Int dimer formation
    • D. Warren, M. D. Sam, +6 authors A. Landy
    • Biology, Medicine
    • Proceedings of the National Academy of Sciences of the United States of America
    • 2003
    • 32
    • PDF
    The Fis protein: it's not just for DNA inversion anymore
    • 207
    Genetic and biochemical analysis of the synaptic complex of invertase Gin.
    • PDF
    Mechanism of chromosome compaction and looping by the Escherichia coli nucleoid protein Fis.
    • 124
    Crystal structure of the nucleoid-associated protein Fis (PA4853) from Pseudomonas aeruginosa.


    Crystallization of the DNA-binding Escherichia coli protein FIS.
    • 4
    Gin-mediated DNA inversion: product structure and the mechanism of strand exchange.
    • 55
    • PDF
    The helix-turn-helix DNA binding motif.
    • 520
    • PDF