TY  - JOUR
AU  - Sievers, Katharina
AU  - Neumann, Piotr
AU  - Sušac, Lukas
AU  - Da Vela, Stefano
AU  - Graewert, Melissa
AU  - Trowitzsch, Simon
AU  - Svergun, Dmitri
AU  - Tampé, Robert
AU  - Ficner, Ralf
TI  - Structural and functional insights into tRNA recognition by human tRNA guanine transglycosylase
JO  - Structure
VL  - 32
IS  - 3
SN  - 0969-2126
CY  - London [u.a.]
PB  - Elsevier Science
M1  - PUBDB-2025-00183
SP  - 316-327.e5
PY  - 2024
N1  - Waiting for fulltext
AB  - 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.
LB  - PUB:(DE-HGF)16
C6  - pmid:38181786
UR  - <Go to ISI:>//WOS:001214900700001
DO  - DOI:10.1016/j.str.2023.12.006
UR  - https://bib-pubdb1.desy.de/record/622097
ER  -