8OMR

Human tRNA guanine transglycosylase (TGT) bound to tRNAAsp

Summary for 8OMR

• Entry DOI: 10.2210/pdb8omr/pdb
• EMDB information: 16976
• Descriptor: Queuine tRNA-ribosyltransferase catalytic subunit 1, Queuine tRNA-ribosyltransferase accessory subunit 2, tRNAAsp, ... (5 entities in total)
• Functional Keywords: rna modification, transglycosylation, nucleid acid-protein complex, trna binding, rna binding protein
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 3
• Total formula weight: 115456.72

Authors

Sievers, K.,Neumann, P.,Susac, L.,Trowitzsch, S.,Tampe, R.,Ficner, R. (deposition date: 2023-03-31, release date: 2023-12-20, Last modification date: 2024-03-20)

Primary citation

Sievers, K.,Neumann, P.,Susac, L.,Da Vela, S.,Graewert, M.,Trowitzsch, S.,Svergun, D.,Tampe, R.,Ficner, R.
Structural and functional insights into tRNA recognition by human tRNA guanine transglycosylase.
Structure, 32:316-, 2024

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 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.

PubMed: 38181786
DOI: 10.1016/j.str.2023.12.006

Experimental method

ELECTRON MICROSCOPY (3.3 Å)