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-Structure paper
タイトル | Structural and functional insights into tRNA recognition by human tRNA guanine transglycosylase. |
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ジャーナル・号・ページ | Structure, Vol. 32, Issue 3, Page 316-327.e5, Year 2024 |
掲載日 | 2024年3月7日 |
著者 | Katharina Sievers / Piotr Neumann / Lukas Sušac / Stefano Da Vela / Melissa Graewert / Simon Trowitzsch / Dmitri Svergun / Robert Tampé / Ralf Ficner / |
PubMed 要旨 | 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. |
リンク | Structure / PubMed:38181786 |
手法 | EM (単粒子) |
解像度 | 3.3 Å |
構造データ | EMDB-16976, PDB-8omr: |
化合物 | ChemComp-ZN: ChemComp-9DG: |
由来 |
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キーワード | RNA BINDING PROTEIN / RNA modification / transglycosylation / nucleid acid-protein complex / tRNA binding |