The adenylyltransferase domain of bacterial Pnkp defines a unique RNA ligase family Journal Article


Authors: Smith, P.; Wang, L. K.; Nair, P. A.; Shuman, S.
Article Title: The adenylyltransferase domain of bacterial Pnkp defines a unique RNA ligase family
Abstract: Pnkp is the end-healing and end-sealing component of an RNA repair system present in diverse bacteria from ten different phyla. To gain insight to the mechanism and evolution of this repair system, we determined the crystal structures of the ligase domain of Clostridium thermocellum Pnkp in three functional states along the reaction pathway: apoenzyme, ligase·ATP substrate complex, and covalent ligase-AMP intermediate. The tertiary structure is composed of a classical ligase nucleotidyltransferase module that is embellished by a unique α-helical insert module and a unique C-terminal α-helical module. Structure-guided mutational analysis identified active site residues essential for ligase adenylylation. Pnkp defines a new RNA ligase family with signature structural and functional properties.
Keywords: unclassified drug; phosphatase; carboxy terminal sequence; mutational analysis; bacteria (microorganisms); crystal structure; models, molecular; crystallization; protein tertiary structure; rna ligase (atp); adenylyltransferase; covalent catalysis; adenylation; nucleotidyltransferase; rna repair; clostridium thermocellum; transferase; enzyme evolution; ligase nucleotidyltransferase; polynucleotide 5' kinase/3' phosphatase
Journal Title: Proceedings of the National Academy of Sciences of the United States of America
Volume: 109
Issue: 7
ISSN: 0027-8424
Publisher: National Academy of Sciences  
Date Published: 2012-02-14
Start Page: 2296
End Page: 2301
Language: English
DOI: 10.1073/pnas.1116827109
PROVIDER: scopus
PMCID: PMC3289333
PUBMED: 22308407
DOI/URL:
Notes: --- - "Export Date: 2 April 2012" - "CODEN: PNASA" - "Source: Scopus"
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  1. Li-Kai Wang
    27 Wang
  2. Stewart H Shuman
    546 Shuman
  3. Pravin A Nair
    12 Nair
  4. Paul M C Smith
    21 Smith