Vaccinia virus DNA topoisomerase: A model eukaryotic type IB enzyme Journal Article
| Author: | Shuman, S. |
| Article Title: | Vaccinia virus DNA topoisomerase: A model eukaryotic type IB enzyme |
| Abstract: | Vaccinia topoisomerase has proven to be an instructive model system for mechanistic studies of the type IB family of DNA topoisomerases. The catalytically relevant functional groups at the active site and the circumferential topoisomerase-DNA interface were correctly surmised by mutational and footprint analysis of vaccinia topoisomerase in advance of structure determinations by X-ray crystallography. It is now evident from multiple crystal structures that the catalytic domains of type IB topoisomerases and site specific recombinases derive from a common ancestral strand transferase capable of forming a DNA-(3'-phosphotyrosyl)-enzyme intermediate. A constellation of conserved amino acids catalyzes attack of the tyrosine nucleophile on the scissile phosphate. Domain dynamics and DNA- induced conformational changes within the catalytic domain are likely to play a role in triggering strand scission and coordinating the strand exchange or strand passage steps. |
| Keywords: | dna-binding proteins; review; nonhuman; protein conformation; protein domain; gene targeting; amino acid sequence; molecular sequence data; sequence homology, amino acid; vaccinia virus; models, molecular; binding sites; virus replication; conformational transition; catalysis; dna binding; x ray crystallography; mutagenesis; transesterification; dna topoisomerase; dna topoisomerases, type i; viral proteins; integrases; virus dna; enzyme metabolism; recombinases; recombinase; dna nucleotidyltransferases; dna footprinting; priority journal; strand passage; tyrosine nucleophile |
| Journal Title: | Biochimica Et Biophysica Acta (BBA) - Gene Structure and Expression |
| Volume: | 1400 |
| Issue: | 1-3 |
| ISSN: | 0167-4781 |
| Publisher: | Elsevier B.V. |
| Date Published: | 1998-10-01 |
| Start Page: | 321 |
| End Page: | 337 |
| Language: | English |
| DOI: | 10.1016/s0167-4781(98)00144-4 |
| PUBMED: | 9748643 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | Review -- Export Date: 12 December 2016 -- Source: Scopus |
