Description
Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:2.9
Classification:RNA
Release Date:2004-10-26
Deposition Date:2004-08-10
Revision Date:2008-04-30#2011-07-13
Molecular Weight:55283.3
Macromolecule Type:RNA
Residue Count:161
Atom Site Count:3372
DOI:10.2210/pdb1u9s/pdb
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-nucleotide specificity domain of an A-type ribonuclease 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.
Resolution:2.9
Classification:RNA
Release Date:2004-10-26
Deposition Date:2004-08-10
Revision Date:2008-04-30#2011-07-13
Molecular Weight:55283.3
Macromolecule Type:RNA
Residue Count:161
Atom Site Count:3372
DOI:10.2210/pdb1u9s/pdb
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-nucleotide specificity domain of an A-type ribonuclease 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.
Date made available | 2004 |
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Publisher | RCSB-PDB |