1s68
Structure and Mechanism of RNA Ligase
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OverviewOverview
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.
About this StructureAbout this Structure
1S68 is a Single protein structure of sequence from Bacteriophage t4 with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Structure and mechanism of RNA ligase., Ho CK, Wang LK, Lima CD, Shuman S, Structure. 2004 Feb;12(2):327-39. PMID:14962393
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