Closing the gap on DNA ligase Journal Article
| Author: | Shuman, S. |
| Article Title: | Closing the gap on DNA ligase |
| Abstract: | The crystal structure of T7 DNA ligase complexed with ATP illuminates the mechanism of covalent catalysis by a superfamily of nucleotidyl transferases that includes the ATP-dependent polynucleotide ligases and the GTP-dependent mRNA capping enzymes. © Current Biology Ltd. |
| Keywords: | genetics; review; molecular genetics; protein conformation; metabolism; chemistry; amino acid sequence; conserved sequence; molecular sequence data; nucleotide sequence; binding site; models, molecular; crystallography, x-ray; binding sites; chemical structure; adenosine triphosphate; x ray crystallography; polydeoxyribonucleotide synthase; dna ligases; nucleotidyltransferase; nucleotidyltransferases; polydeoxyribonucleotide synthase (atp) |
| Journal Title: | Structure |
| Volume: | 4 |
| Issue: | 6 |
| ISSN: | 0969-2126 |
| Publisher: | Cell Press |
| Date Published: | 1996-06-01 |
| Start Page: | 653 |
| End Page: | 656 |
| Language: | English |
| DOI: | 10.1016/s0969-2126(96)00070-6 |
| PUBMED: | 8805556 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | Review -- Export Date: 22 November 2017 -- Source: Scopus |
