Domain structure of vaccinia DNA ligase Journal Article
| Authors: | Sekiguchi, J.; Shuman, S. |
| Article Title: | Domain structure of vaccinia DNA ligase |
| Abstract: | The 552 amino acid vaccinia virus DNA ligase consists of three structural domains defined by partial proteolysis: (i) an amino-terminal 175 amino acid segment that is susceptible to digestion with chymotrypsin and trypsin; (ii) a protease-resistant central domain that contains the active site of nucleotidyl transfer (Lys-231); (iii) a protease-resistant carboxyl domain. The two protease-resistant domains are separated by a protease-sensitive interdomain bridge from positions 296 to 307. Adenylyltransferase and DNA ligation activities are preserved when the N-terminal 200 amino acids are deleted. However, the truncated form of vaccinia ligase has a reduced catalytic rate in strand joining and a lower affinity for DNA than does the full-sized enzyme. The 350 amino acid catalytic core of the vaccinia ligase is similar in size and protease-sensitivity to the full-length bacteriophage T7 DNA ligase. |
| Keywords: | controlled study; sequence deletion; nonhuman; binding affinity; protein domain; carboxy terminal sequence; protein degradation; protein binding; enzyme activity; structure activity relation; dna; amino acid sequence; molecular sequence data; amino terminal sequence; kinetics; recombinant proteins; vaccinia virus; dna, viral; protein structure, tertiary; adenosine triphosphate; polydeoxyribonucleotide synthase; enzyme structure; enzyme substrate complex; hydrolysis; chymotrypsin; virus protein; dna ligases; enzyme active site; trypsin; endopeptidases; vaccinia; nucleotidyltransferases; transferase; priority journal; article; bacteriophage t7 |
| Journal Title: | Nucleic Acids Research |
| Volume: | 25 |
| Issue: | 4 |
| ISSN: | 0305-1048 |
| Publisher: | Oxford University Press |
| Date Published: | 1997-02-15 |
| Start Page: | 727 |
| End Page: | 734 |
| Language: | English |
| DOI: | 10.1093/nar/25.4.727 |
| PUBMED: | 9016621 |
| PROVIDER: | scopus |
| PMCID: | PMC146513 |
| DOI/URL: | |
| Notes: | Article -- Export Date: 17 March 2017 -- Source: Scopus |
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