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Crystal Structure of a Self-Spliced Group II Intron
Navtej Toor,1*Kevin S. Keating,2Sean D. Taylor,3Anna Marie Pyle1,4*
Group II introns are self-splicing ribozymes that catalyze theirown excision from precursor transcripts and insertion into newgenetic locations. Here we report the crystal structure of anintact, self-spliced group II intron from Oceanobacillus iheyensisat 3.1 angstrom resolution. An extensive network of tertiaryinteractions facilitates the ordered packing of intron subdomainsaround a ribozyme core that includes catalytic domain V. Thebulge of domain V adopts an unusual helical structure that islocated adjacent to a major groove triple helix (catalytic triplex).The bulge and catalytic triplex jointly coordinate two divalentmetal ions in a configuration that is consistent with a two–metalion mechanism for catalysis. Structural and functional analogiessupport the hypothesis that group II introns and the spliceosomeshare 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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[DOI: 10.1126/science.1156721] |Summary »|Full Text »|PDF »
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