Structure and mechanism of T4 polynucleotide kinase: An RNA repair enzyme Journal Article
| Authors: | Wang, L. K.; Lima, C. D.; Shuman, S. |
| Article Title: | Structure and mechanism of T4 polynucleotide kinase: An RNA repair enzyme |
| Abstract: | T4 polynucleotide kinase (Pnk), in addition to being an invaluable research tool, exemplifies a family of bifunctional enzymes with 5′-kinase and 3′-phosphatase activities that play key roles in RNA and DNA repair. T4 Pnk is a homotetramer composed of a C-terminal phosphatase domain and an N-terminal kinase domain. The 2.0 Å crystal structure of the isolated kinase domain highlights a tunnel-like active site through the heart of the enzyme, with an entrance on the 5′ OH acceptor side that can accommodate a single-stranded polynucleotide. The active site is composed of essential side chains that coordinate the β phosphate of the NTP donor and the 3′ phosphate of the 5′ OH acceptor, plus a putative general acid that activates the 5′ OH. The structure rationalizes the different specificities of T4 and eukaryotic Pnk and suggests a model for the assembly of the tetramer. |
| Keywords: | nonhuman; mutant protein; protein domain; phosphatase; enzyme activity; rna; amino acid sequence; molecular sequence data; sequence homology, amino acid; eukaryota; crystal structure; models, molecular; binding sites; catalysis; enzyme specificity; enzyme structure; protein structure, quaternary; phosphotransferase; polynucleotide 5' hydroxyl kinase; polynucleotide 5'-hydroxyl-kinase; enzyme mechanism; tetramer; enzyme active site; nucleotide; polynucleotide kinase; rna repair; protein quaternary structure; bacteriophage t4; priority journal; article; bacteriophage t4/3′ phosphatase |
| Journal Title: | EMBO Journal |
| Volume: | 21 |
| Issue: | 14 |
| ISSN: | 0261-4189 |
| Publisher: | Wiley Blackwell |
| Date Published: | 2002-07-15 |
| Start Page: | 3873 |
| End Page: | 3880 |
| Language: | English |
| DOI: | 10.1093/emboj/cdf397 |
| PUBMED: | 12110598 |
| PROVIDER: | scopus |
| PMCID: | PMC126130 |
| DOI/URL: | |
| Notes: | Export Date: 14 November 2014 -- Source: Scopus |
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