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@ARTICLE{Oberthuer:97417,
      author       = {Oberthuer, D. and Eichert, A. and Erdmann, V. A. and
                      Fuerste, J. P. and Betzel, C. and Foerster, C. and DESY},
      title        = {{T}he crystal structure of a {T}hermus thermophilus
                      t{RNA}({G}ly) acceptor stem microhelix at 1.6{A}mper
                      resolution.},
      journal      = {Biochemical and biophysical research communications},
      volume       = {404},
      issn         = {0006-291X},
      address      = {Orlando, Fla.},
      publisher    = {Academic Press},
      reportid     = {PHPPUBDB-20397},
      pages        = {245-249},
      year         = {2011},
      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.},
      keywords     = {Base Sequence / Crystallography, X-Ray / Glycine-tRNA
                      Ligase: metabolism / Nucleic Acid Conformation / RNA,
                      Transfer, Gly: chemistry / RNA, Transfer, Gly: metabolism /
                      Thermus thermophilus: metabolism / RNA, Transfer, Gly (NLM
                      Chemicals) / Glycine-tRNA Ligase (NLM Chemicals)},
      cin          = {EMBL},
      ddc          = {570},
      cid          = {$I:(DE-H253)EMBL_-2012_-20130307$},
      pnm          = {DORIS Beamline K1.1 (POF2-54G13)},
      pid          = {G:(DE-H253)POF2-K1.1-20130405},
      experiment   = {EXP:(DE-H253)D-K1.1-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:21114959},
      UT           = {WOS:000286487700044},
      doi          = {10.1016/j.bbrc.2010.11.101},
      url          = {https://bib-pubdb1.desy.de/record/97417},
}