Abstract
Large RNA molecules, such as ribozymes, fold with well-defined tertiary structures that are important for their activity. There are many instances of ribozymes with identical function but differences in their secondary structures, suggesting alternative tertiary folds. Here, we report a crystal structure of the 161-nucteotide specificity domain of an A-type ribonuctease P that differs in secondary and tertiary structure from the specificity domain of a B-type molecule. Despite the differences, the cores of the domains have similar three-dimensional structure. Remarkably, the similar geometry of the cores is stabilized by a different set of interactions involving distinct auxiliary elements.
Original language | English (US) |
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Pages (from-to) | 104-107 |
Number of pages | 4 |
Journal | Science |
Volume | 306 |
Issue number | 5693 |
DOIs | |
State | Published - Oct 1 2004 |
ASJC Scopus subject areas
- General
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Crystal structure of the specificity domain of Ribonuclease P of the A-type
Krasilnikov, A. S. (Contributor), Xiao, Y. (Contributor), Pan, T. (Contributor) & Mondragon, A. (Contributor), Protein Data Bank (PDB), Oct 26 2004
DOI: 10.2210/pdb1U9S/pdb, https://www.wwpdb.org/pdb?id=pdb_00001u9s
Dataset