Crystal structure of tRNAHis guanylyltransferase from Saccharomyces cerevisiae

Kitaik Lee, Eun Hye Lee, Jonghyeon Son, Kwang Yeon Hwang

Research output: Contribution to journalArticlepeer-review

4 Citations (Scopus)


tRNA maturation involves several steps, including processing, splicing, CCA addition, and posttranscriptional modifications. tRNAHis guanylyltransferase (Thg1) is the only enzyme known to catalyze templated nucleotide addition in the 3′–5′ direction, unlike other DNA and RNA polymerases. For a better understanding of its unique catalytic mechanism at the molecular level, we determined the crystal structure of GTP-bound Thg1 from Saccharomyces cerevisiae at the maximum resolution of 3.0 Å. The structure revealed the enzyme to have a tetrameric conformation that is well conserved among different species, and the GTP molecule was clearly bound at the active site, coordinating with two magnesium ions. In addition, two flexible protomers at the potential binding site (PBS) for tRNAHis were observed. We suggest that the PBS of the tetramer could also be one of the sites for interaction with partner proteins.

Original languageEnglish
Pages (from-to)400-405
Number of pages6
JournalBiochemical and biophysical research communications
Issue number2
Publication statusPublished - 2017 Aug 19


  • GTP
  • Posttranscriptional modifications
  • Reverse polymerization
  • Thg1
  • X-ray structure

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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