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TitleStructural and functional insights into tRNA recognition by human tRNA guanine transglycosylase.
Journal, issue, pagesStructure, Vol. 32, Issue 3, Page 316-327.e5, Year 2024
Publish dateMar 7, 2024
AuthorsKatharina Sievers / Piotr Neumann / Lukas Sušac / Stefano Da Vela / Melissa Graewert / Simon Trowitzsch / Dmitri Svergun / Robert Tampé / Ralf Ficner /
PubMed AbstractEukaryotic tRNA guanine transglycosylase (TGT) is an RNA-modifying enzyme which catalyzes the base exchange of the genetically encoded guanine 34 of tRNAs for queuine, a hypermodified 7-deazaguanine ...Eukaryotic tRNA guanine transglycosylase (TGT) is an RNA-modifying enzyme which catalyzes the base exchange of the genetically encoded guanine 34 of tRNAs 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.
External linksStructure / PubMed:38181786
MethodsEM (single particle)
Resolution3.3 Å
Structure data

16976

8omr

EMDB-16976, PDB-8omr:
Human tRNA guanine transglycosylase (TGT) bound to tRNAAsp
Method: EM (single particle) / Resolution: 3.3 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-9DG:
9-DEAZAGUANINE

Source
  • homo sapiens (human)
KeywordsRNA BINDING PROTEIN / RNA modification / transglycosylation / nucleid acid-protein complex / tRNA binding

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