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TitleCryo-EM reveals that tRNA-transglycosylase can bind and act upon two tRNAs.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 123, Issue 30, Page e2601895123, Year 2026
Publish dateJul 28, 2026
AuthorsAlexander Harjung / Ember M Ruth / Mariusz Matyszewski / Jaehee Park / Caroline Knittel / Evan McCormack / Neal K Devaraj /
PubMed AbstractBacterial tRNA-guanine transglycosylases (TGT) are essential enzymes involved in tRNA modification, contributing to the virulence of multiple pathogens. TGT from was the first protein of this family ...Bacterial tRNA-guanine transglycosylases (TGT) are essential enzymes involved in tRNA modification, contributing to the virulence of multiple pathogens. TGT from was the first protein of this family to be isolated and purified, and as such has served as a model enzyme for the biochemical characterization of TGTs. TGT is also one of the most disease-relevant TGTs, sharing high sequence identity with TGTs from several human pathogenic bacteria, including spp. and spp. Notably, TGTs from some strains are sequence-identical to the enzyme. In addition, as a highly promiscuous enzyme, TGT has found use as an RNA-modification tool in chemical biology, enabling site-specific covalent RNA modification in vitro and in vivo. For these reasons, there has been significant interest in solving the structure of TGT. However, crystallization of TGT has proven difficult, and to date, structural insights have relied on surrogate TGT enzymes from other organisms. Here, we present the cryo-EM structure of TGT and its covalent intermediate with a full-length tRNA. Unexpectedly, the structure reveals that the TGT dimer binds and acts upon two tRNAs, which is unlike all other known TGTs. Closer analysis of the TGT-tRNA complex reveals several important interactions outside of the enzyme's active site, that facilitate RNA binding and stabilize the conformational change of the tRNA anticodon loop. Based on these structural insights, we were able to design improved, high-affinity, TGT substrate RNA hairpins.
External linksProc Natl Acad Sci U S A / PubMed:42479844
MethodsEM (single particle)
Resolution2.72 - 3.52 Å
Structure data

75124

10fa

EMDB-75124, PDB-10fa:
E. coli tRNA guanine transgylcosylase
Method: EM (single particle) / Resolution: 3.52 Å

75125

10fb

EMDB-75125, PDB-10fb:
E. coli TGT covalent intermediate with 1 tRNA
Method: EM (single particle) / Resolution: 3.01 Å

75126

10fc

EMDB-75126, PDB-10fc:
E. coli TGT covalent intermediate with 2 tRNAs
Method: EM (single particle) / Resolution: 2.72 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-9DG:
9-DEAZAGUANINE

Source
  • escherichia coli (E. coli)
KeywordsTRANSFERASE / TGT / RNA modifying enzyme / TRANSFERASE/RNA / TRANSFERASE-RNA complex

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