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Science 4 April 2008:
Vol. 320. no. 5872, pp. 77 - 82
DOI: 10.1126/science.1153803
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Research Articles

Crystal Structure of a Self-Spliced Group II Intron

Navtej Toor,1* Kevin S. Keating,2 Sean D. Taylor,3 Anna Marie Pyle1,4*

Group II introns are self-splicing ribozymes that catalyze their own excision from precursor transcripts and insertion into new genetic locations. Here we report the crystal structure of an intact, self-spliced group II intron from Oceanobacillus iheyensis at 3.1 angstrom resolution. An extensive network of tertiary interactions facilitates the ordered packing of intron subdomains around a ribozyme core that includes catalytic domain V. The bulge of domain V adopts an unusual helical structure that is located adjacent to a major groove triple helix (catalytic triplex). The bulge and catalytic triplex jointly coordinate two divalent metal ions in a configuration that is consistent with a two–metal ion mechanism for catalysis. Structural and functional analogies support the hypothesis that group II introns and the spliceosome share a common ancestor.

1 Department of Molecular Biophysics and Biochemistry, Yale University, 266 Whitney Avenue, Bass Building, New Haven, CT 06511, USA.
2 Interdepartmental Program in Computational Biology and Bioinformatics, Yale University, New Haven, CT 06511, USA.
3 Department of Molecular, Cellular and Developmental Biology, Yale University, New Haven, CT 06511, USA.
4 Howard Hughes Medical Institute, Chevy Chase, MD 20815, USA.

* To whom correspondence should be addressed. E-mail: anna.pyle{at}yale.edu (A.M.P.); navtej.toor{at}yale.edu (N.T.)

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