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Andrey S. Krasilnikov,1Yinghua Xiao,1Tao Pan,2Alfonso Mondragón1*
Large RNA molecules, such as ribozymes, fold with well-definedtertiary structures that are important for their activity. Thereare many instances of ribozymes with identical function butdifferences in their secondary structures, suggesting alternativetertiary folds. Here, we report a crystal structure of the 161-nucleotidespecificity domain of an A-type ribonuclease P that differsin secondary and tertiary structure from the specificity domainof a B-type molecule. Despite the differences, the cores ofthe domains have similar three-dimensional structure. Remarkably,the similar geometry of the cores is stabilized by a differentset of interactions involving distinct auxiliary elements.
1 Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, IL 60208, USA. 2 Department of Biochemistry and Molecular Biology, University of Chicago, 920 East 58th Street, Chicago, IL 60637, USA.
* To whom correspondence should be addressed. E-mail: a-mondragon{at}northwestern.edu
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