A glimpse into the active site of a group II intron and maybe the spliceosome, too.
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.
Dayie
Kwaku T
KT
Department of Molecular Genetics, Lerner Research Institute, Cleveland Clinic, Cleveland, Ohio 44195, USA.
Padgett
Richard A
RA
D017398:Alternative Splicing; D001665:Binding Sites; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D007438:Introns; D007477:Ions / Q000737:chemistry; D008670:Metals / Q000737:chemistry; D009690:Nucleic Acid Conformation; D016337:RNA, Catalytic / Q000737:chemistry* / Q000145:classification; D017381:Spliceosomes / Q000737:chemistry* / Q000201:enzymology*
D007477:Ions; D008670:Metals; D016337:RNA, Catalytic