Crystal structure of tRNA(His) guanylyltransferase from Saccharomyces cerevisiae
- Authors
- Lee, Kitaik; Lee, Eun Hye; Son, Jonghyeon; Hwang, Kwang Yeon
- Issue Date
- 19-8월-2017
- Publisher
- ACADEMIC PRESS INC ELSEVIER SCIENCE
- Keywords
- Thgl; Reverse polymerization; Posttranscriptional modifications; GTP; X-ray structure
- Citation
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.490, no.2, pp.400 - 405
- Indexed
- SCIE
SCOPUS
- Journal Title
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
- Volume
- 490
- Number
- 2
- Start Page
- 400
- End Page
- 405
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/82540
- DOI
- 10.1016/j.bbrc.2017.06.054
- ISSN
- 0006-291X
- Abstract
- tRNA maturation involves several steps, including processing, splicing, CCA addition, and post transcriptional modifications. tRNA(His) guanylyltransferase (Thgl) 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 Thgl from Saccharomyces cerevisiae at the maximum resolution of 3.0 angstrom. 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(His) were observed. We suggest that the PBS of the tetramer could also be one of the sites for interaction with partner proteins. (C) 2017 Elsevier Inc. All rights reserved.
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Collections - Graduate School > Department of Biotechnology > 1. Journal Articles
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