Structure and mechanism of RNA ligase Journal Article

  


Authors: Ho, C. K.; Wang, L. K.; Lima, C. D.; Shuman, S.
Article Title: Structure and mechanism of RNA ligase
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′-PO 4 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 Å 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.
Keywords: controlled study; mutation; nonhuman; protein domain; animals; carboxy terminal sequence; protein binding; trypanosoma; molecular evolution; amino acid sequence; molecular sequence data; sequence homology, amino acid; messenger rna; crystal structure; models, molecular; crystallography, x-ray; protein structure, tertiary; catalysis; protein folding; polydeoxyribonucleotide synthase; enzyme binding; rna ligase (atp); enzyme mechanism; viral proteins; enzyme active site; adenosine phosphate; adenosine monophosphate; rna ligase; bacteriophage; virus enzyme; bacteriophage t4; leishmania; priority journal; article; unidentified bacteriophage
Journal Title: Structure
Volume: 12
Issue: 2
ISSN: 0969-2126
Publisher: Cell Press  
Date Published: 2004-02-01
Start Page: 327
End Page: 339
Language: English
DOI: 10.1016/j.str.2004.01.011
PROVIDER: scopus
PUBMED: 14962393
DOI/URL:

http://www.scopus.com/inward/record.url?eid=2-s2.0-1242283844&partnerID=40&md5=4717bee4b425d07cb3592be3345dff0d
Notes: Structure -- Cited By (since 1996):72 -- Export Date: 16 June 2014 -- CODEN: STRUE -- Source: Scopus
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MSK Authors
  1. Li-Kai Wang
    27 Wang
  2. Chong-Kiong Ho
    33 Ho
  3. Stewart H Shuman
    546 Shuman
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