5XOX

Crystal structure of tRNA(His) guanylyltranserase from Saccharomyces cerevisiae

Summary for 5XOX

• Entry DOI: 10.2210/pdb5xox/pdb
• Descriptor: tRNA(His) guanylyltransferase, GUANOSINE-5'-TRIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: thg1, reverse polymerization, post-transcriptional modification, gtp, transferase
• Biological source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
• Total number of polymer chains: 6
• Total formula weight: 175058.46

Authors

Lee, K.,Lee, E.H.,Son, J.,Hwang, K.Y. (deposition date: 2017-05-31, release date: 2017-07-12, Last modification date: 2023-11-22)

Primary citation

Lee, K.,Lee, E.H.,Son, J.,Hwang, K.Y.
Crystal structure of tRNA(His) guanylyltransferase from Saccharomyces cerevisiae
Biochem. Biophys. Res. Commun., 490:400-405, 2017

PubMed Abstract: tRNA maturation involves several steps, including processing, splicing, CCA addition, and posttranscriptional modifications. tRNA 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 tRNA were observed. We suggest that the PBS of the tetramer could also be one of the sites for interaction with partner proteins.

PubMed: 28623126
DOI: 10.1016/j.bbrc.2017.06.054

Experimental method

X-RAY DIFFRACTION (3 Å)