%0 Journal Article
%A Sievers, Katharina
%A Neumann, Piotr
%A Sušac, Lukas
%A Da Vela, Stefano
%A Graewert, Melissa
%A Trowitzsch, Simon
%A Svergun, Dmitri
%A Tampé, Robert
%A Ficner, Ralf
%T Structural and functional insights into tRNA recognition by human tRNA guanine transglycosylase
%J Structure
%V 32
%N 3
%@ 0969-2126
%C London [u.a.]
%I Elsevier Science
%M PUBDB-2025-00183
%P 316-327.e5
%D 2024
%Z Waiting for fulltext
%X 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.
%F PUB:(DE-HGF)16
%9 Journal Article
%$ pmid:38181786
%U <Go to ISI:>//WOS:001214900700001
%R 10.1016/j.str.2023.12.006
%U https://bib-pubdb1.desy.de/record/622097