1s68: Difference between revisions

Revision as of 00:27, 28 July 2008

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File:1s68.png

Template:STRUCTURE 1s68

Structure and Mechanism of RNA LigaseStructure and Mechanism of RNA Ligase

Template:ABSTRACT PUBMED 14962393

About this StructureAbout this Structure

1S68 is a Single protein structure of sequence from Enterobacteria phage t4. 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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-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.
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 [[Category: Rna repair]]
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