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1S68

Structure and Mechanism of RNA Ligase

1S68 の概要
エントリーDOI10.2210/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
Ho, C.K.,Wang, L.K.,Lima, C.D.,Shuman, S. (登録日: 2004-01-22, 公開日: 2004-02-24, 最終更新日: 2024-02-14)
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: 14962393
DOI: 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)
構造検証レポート
Validation report summary of 1s68
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2024-11-06に公開中

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