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-Structure paper
Title | Structural and functional insights into tRNA recognition by human tRNA guanine transglycosylase. |
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Journal, issue, pages | Structure, Vol. 32, Issue 3, Page 316-327.e5, Year 2024 |
Publish date | Mar 7, 2024 |
Authors | Katharina Sievers / Piotr Neumann / Lukas Sušac / Stefano Da Vela / Melissa Graewert / Simon Trowitzsch / Dmitri Svergun / Robert Tampé / Ralf Ficner / |
PubMed Abstract | 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 ...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 links | Structure / PubMed:38181786 |
Methods | EM (single particle) |
Resolution | 3.3 Å |
Structure data | EMDB-16976, PDB-8omr: |
Chemicals | ChemComp-ZN: ChemComp-9DG: |
Source |
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Keywords | RNA BINDING PROTEIN / RNA modification / transglycosylation / nucleid acid-protein complex / tRNA binding |