Abstract
Two independent, three-dimensional structures of yeast tRNAAsp, mainly differing by the conformation of the D loop, have been obtained from a multiple isomorphous replacement (MIR) X-ray analysis at 3.5-Å resolution. The folding of the ribose–phosphate backbone is similar to that found for tRNAphe; major differences concern the relative positioning of the acceptor and anticodon stems, and the conformation of the loops in the two molecules. Crystal packing involves self-complementary GUC anticodon interactions.
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Moras, D., Comarmond, M., Fischer, J. et al. Crystal structure of yeast tRNAAsp. Nature 288, 669–674 (1980). https://doi.org/10.1038/288669a0
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DOI: https://doi.org/10.1038/288669a0
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