Download MendeleyCrystal structure of a group I ribozyme domain: principles of RNA packing.
Cate, J.H., Gooding, A.R., Podell, E., Zhou, K., Golden, B.L., Kundrot, C.E., Cech, T.R., Doudna, J.A.(1996) Science 273: 1678-1685
- PubMed: 8781224
- DOI: https://doi.org/10.1126/science.273.5282.1678
- Primary Citation of Related Structures:
1GID - PubMed Abstract:
Group I self-splicing introns catalyze their own excision from precursor RNAs by way of a two-step transesterification reaction. The catalytic core of these ribozymes is formed by two structural domains. The 2.8-angstrom crystal structure of one of these, the P4-P6 domain of the Tetrahymena thermophila intron, is described. In the 160-nucleotide domain, a sharp bend allows stacked helices of the conserved core to pack alongside helices of an adjacent region. Two specific long-range interactions clamp the two halves of the domain together: a two-Mg2+-coordinated adenosine-rich corkscrew plugs into the minor groove of a helix, and a GAAA hairpin loop binds to a conserved 11-nucleotide internal loop. Metal- and ribose-mediated backbone contacts further stabilize the close side-by-side helical packing. The structure indicates the extent of RNA packing required for the function of large ribozymes, the spliceosome, and the ribosome.
Organizational Affiliation:
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA. [email protected]
