Crystal structure of yeast tRNAAsp.
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-A 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.
D001224:Aspartic Acid; D001483:Base Sequence; D008958:Models, Molecular; D009690:Nucleic Acid Conformation; D010649:Phenylalanine; D012331:RNA, Fungal; D012343:RNA, Transfer; D012441:Saccharomyces cerevisiae; D013329:Structure-Activity Relationship; D014961:X-Ray Diffraction
D012331:RNA, Fungal; D001224:Aspartic Acid; D010649:Phenylalanine; D012343:RNA, Transfer