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The structure of I-Crel, a Group I intron-encoded homing endonuclease

Nature Structural Biology volume 4, pages 468–476 (1997)Cite this article

Abstract

The structure of I-Crel provides the first view of a protein encoded by a gene within an intron. This endonuclease recognizes a long DNA site ∼20 base pairs in length and facilitates the lateral transfer of that intron. The protein exhibits a DNA-binding surface consisting of four antiparallel β-strands that form a 20 Å wide groove which is over 70 Å long. The architecture of this fold is different from that of the TATA binding protein, TBP, which also contains an antiparallel β-saddle. The conserved LAGLIDADG motif, which is found in many mobile intron endonucleases, maturases and inteins, forms a novel helical interface and contributes essential residues to the active site.

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Authors and Affiliations

  1. Fred Hutchinson Cancer Research Center, Program in Structural Biology, Division of Basic Sciences, 1124 Columbia Street, Seattle, Washington, 98104, USA

    Patrick J. Heath & Barry L. Stoddard

  2. University of Washington, Department of Pathology, Box 357470, Seattle, Washington, 98195, USA

    Kathryn M. Stephens & Raymond J. Monnat Jr

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  4. Barry L. Stoddard
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Heath, P., Stephens, K., Monnat, R. et al. The structure of I-Crel, a Group I intron-encoded homing endonuclease. Nat Struct Mol Biol 4, 468–476 (1997). https://doi.org/10.1038/nsb0697-468

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