Conservation of structure and mechanism between eukaryotic topoisomerase I and site-specific recombinases Journal Article
| Authors: | Cheng, C.; Kussie, P.; Pavletich, N.; Shuman, S. |
| Article Title: | Conservation of structure and mechanism between eukaryotic topoisomerase I and site-specific recombinases |
| Abstract: | Vaccinia DNA topoisomerase break and rejoins DNA strands through a DNA- (3'-phosphotyrosyl)-enzyme intermediate. A C-terminal catalytic domain, Topo(81-314), suffices for transesterification chemistry. The domain contains a constellation of five amino acids, conserved in all eukaryotic type IB topoisomerases, that catalyzes attack of the tyrosine nucleophile on the scissile phosphate. The structure of the catalytic domain, consisting of ten α helices and a three-strand β sheet, resembles the catalytic domain, consisting of ten α helices and a three-strand β sheet, resembles the catalytic domains of site-specific recombinases that act via a topoisomerase IB-like mechanism. The topoisomerase catalytic pentad is conserved in the tertiary structures of the recombinases despite scant sequence similarity overall. This implies that the catalytic domains of type IB topoisomerases and recombinases derive from a common ancestral strand transferase. |
| Keywords: | nonhuman; structure activity relation; amino acid sequence; molecular sequence data; sequence homology, amino acid; saccharomyces cerevisiae; eukaryota; protein structure, tertiary; binding sites; enzyme structure; protein structure, secondary; genetic conservation; eukaryote; dna topoisomerase; dna topoisomerases, type i; viral proteins; integrases; vaccinia; recombinase; eukaryotic cells; priority journal; article |
| Journal Title: | Cell |
| Volume: | 92 |
| Issue: | 6 |
| ISSN: | 0092-8674 |
| Publisher: | Cell Press |
| Date Published: | 1998-03-20 |
| Start Page: | 841 |
| End Page: | 850 |
| Language: | English |
| DOI: | 10.1016/s0092-8674(00)81411-7 |
| PUBMED: | 9529259 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | Article -- Export Date: 12 December 2016 -- Source: Scopus |
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