A magnesium ion core at the heart of a ribozyme domain
- 1 July 1997
- journal article
- research article
- Published by Springer Nature in Nature Structural & Molecular Biology
- Vol. 4 (7) , 553-558
- https://doi.org/10.1038/nsb0797-553
Abstract
Large ribozymes require divalent metal ions to fold. We show here that the tertiary structure of the Tetrahymena group I intron P4-P6 domain nucleates around a magnesium ion core. In the domain crystal structure, five magnesium ions bind in a three-helix junction at the centre of the molecule. Single atom changes in any one of four magnesium sites in this three-helix junction destroy folding of the entire 160-nucleotide P4-P6 domain. The magnesium ion core may be the RNA counterpart to the protein hydrophobic core, burying parts of the RNA molecule in the native structure.Keywords
This publication has 39 references indexed in Scilit:
- Capturing the Structure of a Catalytic RNA Intermediate: The Hammerhead RibozymeScience, 1996
- Three-dimensional structure of a hammerhead ribozymeNature, 1994
- Kinetic Intermediates in RNA FoldingScience, 1994
- Ribozymes: A Distinct Class of MetalloenzymesScience, 1993
- Thermal unfolding of a group I ribozyme: the low-temperature transition is primarily disruption of tertiary structureBiochemistry, 1993
- Visualizing the Higher Order Folding of a Catalytic RNA MoleculeScience, 1991
- Modelling of the three-dimensional architecture of group I catalytic introns based on comparative sequence analysisJournal of Molecular Biology, 1990
- Dominant forces in protein foldingBiochemistry, 1990
- A nuclear magnetic resonance study of secondary and tertiary structure in yeast tRNAPheBiochemistry, 1977
- Conformational changes of transfer ribonucleic acid. Equilibrium phase diagramsBiochemistry, 1972