Crystal Structure of a Group I Ribozyme Domain: Principles of RNA Packing
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- Jamie H. Cate
- 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;
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- Anne R. Gooding
- 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;
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- Elaine Podell
- 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;
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- Kaihong Zhou
- 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;
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- Barbara L. Golden
- 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;
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- Craig E. Kundrot
- 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;
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- Thomas R. Cech
- 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;
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- Jennifer A. Doudna
- 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;
Abstract
<jats:p> 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 <jats:italic>Tetrahymena thermophila</jats:italic> 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-Mg <jats:sup>2+</jats:sup> -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. </jats:p>
Journal
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- Science
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Science 273 (5282), 1678-1685, 1996-09-20
American Association for the Advancement of Science (AAAS)
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Details 詳細情報について
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- CRID
- 1362544420434029824
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- ISSN
- 10959203
- 00368075
- http://id.crossref.org/issn/00368075
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- Data Source
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- Crossref