Crystal structure of a phage Twort group I ribozyme–product complex
- 5 December 2004
- journal article
- Published by Springer Science and Business Media LLC in Nature Structural & Molecular Biology
- Vol. 12 (1), 82-89
- https://doi.org/10.1038/nsmb868
Abstract
Group I introns are catalytic RNAs capable of orchestrating two sequential phosphotransesterification reactions that result in self-splicing. To understand how the group I intron active site facilitates catalysis, we have solved the structure of an active ribozyme derived from the orf142-I2 intron from phage Twort bound to a four-nucleotide product RNA at a resolution of 3.6 Å. In addition to the three conserved domains characteristic of all group I introns, the Twort ribozyme has peripheral insertions characteristic of phage introns. These elements form a ring that completely envelops the active site, where a snug pocket for guanosine is formed by a series of stacked base triples. The structure of the active site reveals three potential binding sites for catalytic metals, and invokes a role for the 2′ hydroxyl of the guanosine substrate in organization of the active site for catalysis.Keywords
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