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@ARTICLE{Sievers:622097,
      author       = {Sievers, Katharina and Neumann, Piotr and Sušac, Lukas and
                      Da Vela, Stefano and Graewert, Melissa and Trowitzsch, Simon
                      and Svergun, Dmitri and Tampé, Robert and Ficner, Ralf},
      title        = {{S}tructural and functional insights into t{RNA}
                      recognition by human t{RNA} guanine transglycosylase},
      journal      = {Structure},
      volume       = {32},
      number       = {3},
      issn         = {0969-2126},
      address      = {London [u.a.]},
      publisher    = {Elsevier Science},
      reportid     = {PUBDB-2025-00183},
      pages        = {316-327.e5},
      year         = {2024},
      note         = {Waiting for fulltext},
      abstract     = {Eukaryotic tRNA guanine transglycosylase (TGT) is an
                      RNA-modifying enzyme which catalyzes the base exchange of
                      the genetically encoded guanine 34 of tRNAsAsp,Asn,His,Tyr
                      for queuine, a hypermodified 7-deazaguanine derivative.
                      Eukaryotic TGT is a heterodimer comprised of a catalytic and
                      a non-catalytic subunit. While binding of the tRNA anticodon
                      loop to the active site is structurally well understood, the
                      contribution of the non-catalytic subunit to tRNA binding
                      remained enigmatic, as no complex structure with a complete
                      tRNA was available. Here, we report a cryo-EM structure of
                      eukaryotic TGT in complex with a complete tRNA, revealing
                      the crucial role of the non-catalytic subunit in tRNA
                      binding. We decipher the functional significance of these
                      additional tRNA-binding sites, analyze solution state
                      conformation, flexibility, and disorder of apo TGT, and
                      examine conformational transitions upon tRNA binding.},
      cin          = {DOOR ; HAS-User / EMBL},
      ddc          = {540},
      cid          = {I:(DE-H253)HAS-User-20120731 / I:(DE-H253)EMBL-20120731},
      pnm          = {6G3 - PETRA III (DESY) (POF4-6G3) / DFG project
                      G:(GEPRIS)390729940 - EXC 2067: Multiscale Bioimaging: Von
                      molekularen Maschinen zu Netzwerken erregbarer Zellen
                      (390729940) / EditMHC - How MHC-I editing complexes shape
                      the hierarchical immune response (789121) / SFB 860 Z01 -
                      Zentrale Einrichtung für Kristallisationsexperimente (Z01)
                      (174684579) / SFB 860 A02 - Kristallographische Studien an
                      molekularen Motoren des Spleißosoms (A02) (174570643) / SFB
                      1565 P09 - Strukturelle und mechanistische Analyse des
                      nukleozytoplasmatischen Transports von RNAs (P09)
                      (515953039)},
      pid          = {G:(DE-HGF)POF4-6G3 / G:(GEPRIS)390729940 /
                      G:(EU-Grant)789121 / G:(GEPRIS)174684579 /
                      G:(GEPRIS)174570643 / G:(GEPRIS)515953039},
      experiment   = {EXP:(DE-H253)P-P12-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:38181786},
      UT           = {WOS:001214900700001},
      doi          = {10.1016/j.str.2023.12.006},
      url          = {https://bib-pubdb1.desy.de/record/622097},
}