Three-Dimensional Structure of Yeast Phenylalanine Transfer RNA: Folding of the Polynucleotide Chain

S. H. Kim(Massachusetts Institute of Technology), Gary J. Quigley(Massachusetts Institute of Technology), F. L. Suddath(Massachusetts Institute of Technology), Alexander McPherson(Massachusetts Institute of Technology), D. Sneden(Massachusetts Institute of Technology), J. J. Kim(Massachusetts Institute of Technology), J. Weinzierl(Massachusetts Institute of Technology), Alexander Rich(Massachusetts Institute of Technology)
Science
January 19, 1973
Cited by 418

Abstract

At 4 A resolution the polynucleotides in yeast phenylalanine transfer RNA are seen in a series of electron dense masses about 5.8 A apart. These peaks are probably associated with the phosphate groups, while lower levels of electron density between segments of adjacent polynucleotide chains are interpreted as arising from hydrogen-bonded purine-pyrimidine base pairs. It is possible to trace the entire polynucleotide chain with only two minor regions of ambiguity. The polynucleotide chain has a secondary structure consistent with the cloverleaf conformation; however, its folding is different from that proposed in any model. The molecule is made of two double-stranded helical regions oriented at right angles to each other in the shape of an L. One end of the L has the CCA acceptor; the anticodon loop is at the other end, and the dihydrouridine and TpsiC loops form the corner.


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