The crystal structure of a Thermus thermophilus tRNA(Gly) acceptor stem microhelix at 1.6Amper resolution.

Oberthuer, D.; Eichert, A.; Erdmann, V. A.; Fuerste, J. P.; Foerster, C.; Betzel, C.

doi:10.1016/j.bbrc.2010.11.101

Journal Article

PHPPUBDB-20397

The crystal structure of a Thermus thermophilus tRNA(Gly) acceptor stem microhelix at 1.6Amper resolution.

Oberthuer, D. ; Eichert, A. ; Erdmann, V. A. ; Fuerste, J. P. ; Betzel, C. ; Foerster, C. ; DESY

2011
Academic Press Orlando, Fla.

Biochemical and biophysical research communications 404, 245-249 (2011) [10.1016/j.bbrc.2010.11.101]

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Please use a persistent id in citations: doi:10.1016/j.bbrc.2010.11.101

Abstract: tRNAs are aminoacylated with the correct amino acid by the cognate aminoacyl-tRNA synthetase. The tRNA/synthetase systems can be divided into two classes: class I and class II. Within class I, the tRNA identity elements that enable the specificity consist of complex sequence and structure motifs, whereas in class II the identity elements are assured by few and simple determinants, which are mostly located in the tRNA acceptor stem. The tRNA(Gly)/glycyl-tRNA-synthetase (GlyRS) system is a special case regarding evolutionary aspects. There exist two different types of GlyRS, namely an archaebacterial/human type and an eubacterial type, reflecting the evolutionary divergence within this system. We previously reported the crystal structures of an Escherichia coli and of a human tRNA(Gly) acceptor stem microhelix. Here we present the crystal structure of a thermophilic tRNA(Gly) aminoacyl stem from Thermus thermophilus at 1.6Å resolution and provide insight into the RNA geometry and hydration.

Keyword(s): Base Sequence (MeSH) ; Crystallography, X-Ray (MeSH) ; Glycine-tRNA Ligase: metabolism (MeSH) ; Nucleic Acid Conformation (MeSH) ; RNA, Transfer, Gly: chemistry (MeSH) ; RNA, Transfer, Gly: metabolism (MeSH) ; Thermus thermophilus: metabolism (MeSH) ; RNA, Transfer, Gly ; Glycine-tRNA Ligase