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Kinked DNA in crystalline complex with EcoRI endonuclease

Nature volume 309, pages 327–331 (1984)Cite this article

Abstract

The 3 Å electron density map of a co-crystalline recognition complex between EcoRI endonuclease and the oligonucleotide TCGCGAATTCGCG reveals that a tight, complementary interface between the enzyme and the major groove of the DNA is the major determinant of sequence specificity. The DNA contains a torsional kink and other departures from the B conformation which unwind the DNA and thereby widen the major groove in the recognition site.

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Authors and Affiliations

  1. Department of Biological Science, University of Pittsburgh, Pittsburgh, Pennsylvania, 15260, USA

    Christin A. Frederick, John Grable, Michele Melia, Cleopas Samudzi, Linda Jen-Jacobson & John M. Rosenberg

  2. Biocrystallography Laboratory, VA Medical Center, Box 12055, Pittsburgh, Pennsylvania, 15240, USA

    Bi-Cheng Wang

  3. Department of Biochemistry and Biophysics, University of California, San Francisco, California, 94143, USA

    Patricia Greene & Herbert W. Boyer

Authors
  1. Christin A. Frederick
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  2. John Grable
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  3. Michele Melia
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  4. Cleopas Samudzi
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Frederick, C., Grable, J., Melia, M. et al. Kinked DNA in crystalline complex with EcoRI endonuclease. Nature 309, 327–331 (1984). https://doi.org/10.1038/309327a0

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