TY - JOUR
T1 - Crystal structure of tRNAHis guanylyltransferase from Saccharomyces cerevisiae
AU - Lee, Kitaik
AU - Lee, Eun Hye
AU - Son, Jonghyeon
AU - Hwang, Kwang Yeon
N1 - Funding Information:
We thank the supporting staff of beamline NW12A of the Photon Factory (Tsukuba, Japan) and beamline 5C-SBII of Pohang Accelerator Light Source (Pohang, Korea) for their help with the data collection. This work was supported by grants from the National Research Foundation of Korea (2017R1A2B2005666). KYH was supported by Korea University grants.
Publisher Copyright:
© 2017 Elsevier Inc.
Copyright:
Copyright 2017 Elsevier B.V., All rights reserved.
PY - 2017/8/19
Y1 - 2017/8/19
N2 - 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.
AB - 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.
KW - GTP
KW - Posttranscriptional modifications
KW - Reverse polymerization
KW - Thg1
KW - X-ray structure
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U2 - 10.1016/j.bbrc.2017.06.054
DO - 10.1016/j.bbrc.2017.06.054
M3 - Article
C2 - 28623126
AN - SCOPUS:85020769669
VL - 490
SP - 400
EP - 405
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 2
ER -