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Author(s)Cate JH; Gooding AR; Podell E; Zhou KH; Golden BL; Kundrot CE; Cech TR; Doudna JA
TitleCrystal structure of a group I ribozyme domain: Principles of RNA packing
SourceSCIENCE 273 (5282): 1678-1685
Date1996 SEP 20
TypeJournal : Article
LCR20   NCR: 70   LCS172   GCS: 728
Comment 
AddressUNIV COLORADO,DEPT CHEM & BIOCHEM,BOULDER,CO 80309.
YALE UNIV,DEPT MOL BIOPHYS & BIOCHEM,NEW HAVEN,CT 06520.
UNIV COLORADO,HOWARD HUGHES MED INST,BOULDER,CO 80309.
AbstractGroup 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-nucleolide 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.
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