TY  - JOUR
AU  - Oberthuer, D.
AU  - Eichert, A.
AU  - Erdmann, V. A.
AU  - Fuerste, J. P.
AU  - Betzel, C.
AU  - Foerster, C.
AU  - DESY
TI  - The crystal structure of a Thermus thermophilus tRNA(Gly) acceptor stem microhelix at 1.6Amper resolution.
JO  - Biochemical and biophysical research communications
VL  - 404
SN  - 0006-291X
CY  - Orlando, Fla.
PB  - Academic Press
M1  - PHPPUBDB-20397
SP  - 245-249
PY  - 2011
AB  - 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.
KW  - Base Sequence
KW  - Crystallography, X-Ray
KW  - Glycine-tRNA Ligase: metabolism
KW  - Nucleic Acid Conformation
KW  - RNA, Transfer, Gly: chemistry
KW  - RNA, Transfer, Gly: metabolism
KW  - Thermus thermophilus: metabolism
KW  - RNA, Transfer, Gly (NLM Chemicals)
KW  - Glycine-tRNA Ligase (NLM Chemicals)
LB  - PUB:(DE-HGF)16
C6  - pmid:21114959
UR  - <Go to ISI:>//WOS:000286487700044
DO  - DOI:10.1016/j.bbrc.2010.11.101
UR  - https://bib-pubdb1.desy.de/record/97417
ER  -