3OTC
Crystal structure of human tRNAHis guanylyltransferase (Thg1)- Native II
3OTC の概要
エントリーDOI | 10.2210/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 | |
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: 21059936DOI: 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) |
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