Superposition of a tRNASer acceptor stem microhelix into the seryl-tRNA synthetase complex

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 tRNA(Ser) to determine the amino acid specificity. tRNA(Ser) acceptor stem microhelices can be aminoacylated with serine,...

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Veröffentlicht in:	Biochemical and biophysical research communications 2007-10, Vol.362 (2), p.415-418
Hauptverfasser:	Förster, C, Brauer, A B E, Fürste, J P, Betzel, Ch, Weber, M, Cordes, F, Erdmann, V A
Format:	Artikel
Sprache:	eng
Schlagworte:	Anticodon - chemistry Anticodon - metabolism Crystallization Crystallography, X-Ray Models, Molecular Nucleic Acid Conformation Protein Binding RNA, Transfer, Amino Acyl - chemistry RNA, Transfer, Amino Acyl - metabolism RNA, Transfer, Ser - chemistry RNA, Transfer, Ser - metabolism Serine-tRNA Ligase - chemistry Serine-tRNA Ligase - metabolism
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Beschreibung
Zusammenfassung:	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 tRNA(Ser) to determine the amino acid specificity. tRNA(Ser) 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 tRNA(Ser)-seryl-tRNA synthetase complex. A 1.8A-resolution tRNA(Ser) acceptor stem crystal structure was superimposed to a 2.9A-resolution crystal structure of a tRNA(Ser)-seryl-tRNA synthetase complex for a visualization of the binding environment of the tRNA(Ser) microhelix.
ISSN:	0006-291X
DOI:	10.1016/j.bbrc.2007.07.178