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Structural basis of anticodon loop recognition by glutaminyl-tRNA synthetase

Nature volume 352, pages 213–218 (1991)Cite this article

Abstract

The refined crystal structure of Escherichia coli glutaminyl transfer RNA synthetase complexed with transfer RNAGln and ATP reveals that the struc-ture of the anticodon loop of the enzyme-bound tRNAGln differs extensively from that of the known crystal structures of uncomplexed tRNA molecules. The anticodon stem is extended by two non-Watson–Crick base pairs, leaving the three anti-codon bases unpaired and splayed out to bind snugly into three separate complementary pockets in the protein. These interactions suggest that the entire anticodon loop provides essential sites for glutaminyl tRNA synthetase discrimination among tRNA molecules.

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Authors and Affiliations

  1. Departments of Molecular Biophysics and Biochemistry, and Chemistry, and Howard Hughes Medical Institute, Yale University, PO Box 6666, New Haven, Connecticut, 06511, USA

    M. A. Rould, J. J. Perona & T. A. Steitz

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  1. M. A. Rould
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  2. J. J. Perona
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  3. T. A. Steitz
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Rould, M., Perona, J. & Steitz, T. Structural basis of anticodon loop recognition by glutaminyl-tRNA synthetase. Nature 352, 213–218 (1991). https://doi.org/10.1038/352213a0

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