1S68
Structure and Mechanism of RNA Ligase
1S68 の概要
エントリーDOI | 10.2210/pdb1s68/pdb |
分子名称 | RNA Ligase 2, ADENOSINE MONOPHOSPHATE (3 entities in total) |
機能のキーワード | ribonucleic acid ligase, rna repair, t4, ligase |
由来する生物種 | Enterobacteria phage T4 |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 28677.55 |
構造登録者 | |
主引用文献 | Ho, C.K.,Wang, L.K.,Lima, C.D.,Shuman, S. Structure and mechanism of RNA ligase. Structure, 12:327-339, 2004 Cited by PubMed Abstract: T4 RNA ligase 2 (Rnl2) exemplifies an RNA ligase family that includes the RNA editing ligases (RELs) of Trypanosoma and Leishmania. The Rnl2/REL enzymes are defined by essential signature residues and a unique C-terminal domain, which we show is essential for sealing of 3'-OH and 5'-PO4 RNA ends by Rnl2, but not for ligase adenylation or phosphodiester bond formation at a preadenylated AppRNA end. The N-terminal segment Rnl2(1-249) of the 334 aa Rnl2 protein comprises an autonomous adenylyltransferase/AppRNA ligase domain. We report the 1.9 A crystal structure of the ligase domain with AMP bound at the active site, which reveals a shared fold, catalytic mechanism, and evolutionary history for RNA ligases, DNA ligases, and mRNA capping enzymes. PubMed: 14962393DOI: 10.1016/S0969-2126(04)00023-1 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.9 Å) |
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