A glimpse into the active site of a group II intron and maybe the spliceosome, too

Kwaku T. Dayie; Richard A. Padgett

doi:10.1261/rna.1154408

A glimpse into the active site of a group II intron and maybe the spliceosome, too

Kwaku T. Dayie1,2,3 and
Richard A. Padgett1

¹Department of Molecular Genetics, Lerner Research Institute, Cleveland Clinic, Cleveland, Ohio 44195, USA
²Center for Structural Biology, Lerner Research Institute, Cleveland Clinic, Cleveland, Ohio 44195, USA
³Department of Chemistry and Biochemistry, University of Maryland, College Park, Maryland 20742, USA

Abstract

The X-ray crystal structure of an excised group II self-splicing intron was recently solved by the Pyle group. Here we review some of the notable features of this structure and what they may tell us about the catalytic active site of the group II ribozyme and potentially the spliceosome. The new structure validates the central role of domain V in both the structure and catalytic function of the ribozyme and resolves several outstanding puzzles raised by previous biochemical, genetic and structural studies. While lacking both exons as well as the cleavage sites and nucleophiles, the structure reveals how a network of tertiary interactions can position two divalent metal ions in a configuration that is ideal for catalysis.

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Footnotes

Reprint requests to: Richard A. Padgett, Department of Molecular Genetics, Lerner Research Institute, Cleveland Clinic, 9500 Euclid Avenue, Cleveland, OH, 44195, USA; e-mail: padgetr@ccf.org; fax: (216) 444-0512; and Kwaku T. Dayie, Department of Chemistry and Biochemistry, Center for Biomolecular Structure and Organization, University of Maryland, 1115 Biomolecular Sciences Building #296, College Park, MD 20742-3360, USA; e-mail: dayie@umd.edu; fax: (301) 314-9121.
Article published online ahead of print. Article and publication date are at http://www.rnajournal.org/cgi/doi/10.1261/rna.1154408.