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3OTC

Crystal structure of human tRNAHis guanylyltransferase (Thg1)- Native II

3OTC の概要
エントリーDOI10.2210/pdb3otc/pdb
関連するPDBエントリー3OTB 3OTC 3OTD 3OTE
分子名称tRNA(His) guanylyltransferase (1 entity in total)
機能のキーワードguanylyltransferase, polymerase-like palm domain, catalytic carboxylates, transferase
由来する生物種Homo sapiens (human)
細胞内の位置Cytoplasm: Q9NWX6
タンパク質・核酸の鎖数2
化学式量合計63257.88
構造登録者
Hyde, S.J.,Eckenroth, B.E.,Doublie, S. (登録日: 2010-09-11, 公開日: 2010-11-17, 最終更新日: 2024-02-21)
主引用文献Hyde, S.J.,Eckenroth, B.E.,Smith, B.A.,Eberley, W.A.,Heintz, N.H.,Jackman, J.E.,Doublie, S.
tRNAHis guanylyltransferase (THG1), a unique 3'-5' nucleotidyl transferase, shares unexpected structural homology with canonical 5'-3' DNA polymerases.
Proc.Natl.Acad.Sci.USA, 107:20305-20310, 2010
Cited by
PubMed Abstract: All known DNA and RNA polymerases catalyze the formation of phosphodiester bonds in a 5' to 3' direction, suggesting this property is a fundamental feature of maintaining and dispersing genetic information. The tRNA(His) guanylyltransferase (Thg1) is a member of a unique enzyme family whose members catalyze an unprecedented reaction in biology: 3'-5' addition of nucleotides to nucleic acid substrates. The 2.3-Å crystal structure of human THG1 (hTHG1) reported here shows that, despite the lack of sequence similarity, hTHG1 shares unexpected structural homology with canonical 5'-3' DNA polymerases and adenylyl/guanylyl cyclases, two enzyme families known to use a two-metal-ion mechanism for catalysis. The ability of the same structural architecture to catalyze both 5'-3' and 3'-5' reactions raises important questions concerning selection of the 5'-3' mechanism during the evolution of nucleotide polymerases.
PubMed: 21059936
DOI: 10.1073/pnas.1010436107
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (3.01 Å)
構造検証レポート
Validation report summary of 3otc
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-07-23に公開中

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