Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1937219 | Biochemical and Biophysical Research Communications | 2007 | 4 Pages |
Abstract
Aminoacyl-tRNA synthetases catalyze the formation of aminoacyl-tRNAs. Seryl-tRNA synthetase is a class II synthetase, which depends on rather few and simple identity elements in tRNASer to determine the amino acid specificity. tRNASer acceptor stem microhelices can be aminoacylated with serine, which makes this part of the tRNA a valuable tool for investigating the structural motifs in a tRNASer–seryl-tRNA synthetase complex. A 1.8 Å-resolution tRNASer acceptor stem crystal structure was superimposed to a 2.9 Å-resolution crystal structure of a tRNASer–seryl-tRNA synthetase complex for a visualization of the binding environment of the tRNASer microhelix.
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Authors
C. Förster, A.B.E. Brauer, J.P. Fürste, Ch. Betzel, M. Weber, F. Cordes, V.A. Erdmann,