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Science 20 September 1996:
Vol. 273. no. 5282, pp. 1678 - 1685
DOI: 10.1126/science.273.5282.1678
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Research Articles

Crystal Structure of a Group I Ribozyme Domain: Principles of RNA Packing

Jamie H. Cate, Anne R. Gooding, Elaine Podell, Kaihong Zhou, Barbara L. Golden, Craig E. Kundrot, Thomas R. Cech, * Jennifer A. Doudna *

Group I self-splicing introns catalyze their own excision from precursor RNAs by way of a two-step transesterification reaction. The catalytic core of these ribozymes is formed by two structural domains. The 2.8-angstrom crystal structure of one of these, the P4-P6 domain of the Tetrahymena thermophila intron, is described. In the 160-nucleotide domain, a sharp bend allows stacked helices of the conserved core to pack alongside helices of an adjacent region. Two specific long-range interactions clamp the two halves of the domain together: a two-Mg2+-coordinated adenosine-rich corkscrew plugs into the minor groove of a helix, and a GAAA hairpin loop binds to a conserved 11-nucleotide internal loop. Metal- and ribose-mediated backbone contacts further stabilize the close side-by-side helical packing. The structure indicates the extent of RNA packing required for the function of large ribozymes, the spliceosome, and the ribosome.

J. H. Cate, K. Zhou, and J. A. Doudna are in the Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA; e-mail: doudna{at}csb.yale.edu. A. R. Gooding, E. Podell, B. L. Golden, C. E. Kundrot, and T. R. Cech are in the Department of Chemistry and Biochemistry, University of Colorado, Boulder, CO 80309, USA; e-mail: cech{at}stripe.colorado.edu. A. R. Gooding, B. L. Golden, E. Podell, and T. Cech are also with the Howard Hughes Medical Institute at Boulder, CO 80309, USA.
*   To whom correspondence should be addressed.

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