Crystal structure of a self-spliced group II intron.

Publication Type:

Journal Article

Authors:

Toor, Navtej; Keating, Kevin S; Taylor, Sean D; Pyle, Anna Marie

Source:

Science, Volume 320, Issue 5872, p.77-82 (2008)

Keywords:

Allosteric Regulation, Bacillaceae, Base Pairing, Binding Sites, Catalysis, Catalytic Domain, Crystallography, X-Ray, Evolution, Molecular, Introns, Ligands, Magnesium, Models, Molecular, Nucleic Acid Conformation, Phylogeny, RNA Splicing, RNA, Bacterial, RNA, Catalytic, Spliceosomes

Abstract:

<p>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.</p>