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- 中村 彰良
- 産業技術総合研究所生物プロセス研究部門合成生物工学研究グループ
書誌事項
- タイトル別名
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- Crystal Structure of tRNA<sup>His</sup> guanylyltransferase Reveals the Structural Basis of Reverse Nucleotide Polymerization
- ヌクレオチド オ 3'マッタン カラ 5'マッタン ホウコウ エ ト シンチョウ スル コウソ ノ サヨウ ゲンリ
- Crystal Structure of tRNAHis guanylyltransferase Reveals the Structural Basis of Reverse Nucleotide Polymerization
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説明
During tRNA maturation tRNAHis guanylyltransferase (Thg1) catalyzes the untemplated 3'-5' addition of a G to the tRNA 5'-end. This additional guanylate provides the major identity element for histidyl-tRNA synthetase to recognize its cognate tRNAHis. Thg1 is a structural homolog of canonical 5'-3' polymerases. Here, we report the structures of Candida albicans Thg1 with its substrates tRNA, or ATP, or GTP. Two tRNAs bind to the tetrameric enzyme complex, but interaction of three subunits is required for tRNA positioning and catalytic activity. The tRNA substrate enters the Thg1 active site from the opposite direction compared to canonical 5'-3' polymerases, indicating that the directionality of nucleotide polymerization is strongly related to the directionality of substrate access. Structural and biochemical data support a reaction model of Thg1 that catalyzes reverse nucleotide addition.
収録刊行物
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- 日本結晶学会誌
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日本結晶学会誌 56 (6), 399-404, 2014
日本結晶学会
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キーワード
詳細情報 詳細情報について
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- CRID
- 1390001204090024064
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- NII論文ID
- 130004799695
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- NII書誌ID
- AN00188364
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- ISSN
- 18845576
- 03694585
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- NDL書誌ID
- 026031589
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- 本文言語コード
- ja
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- データソース種別
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- JaLC
- NDLサーチ
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- 抄録ライセンスフラグ
- 使用不可
