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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