Conservation of structure and mechanism between eukaryotic topoisomerase I and site-specific recombinases

Chonghui Cheng*, Paul Kussie, Nikola Pavletich, Stewart Shuman

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

213 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)841-850
Number of pages10
JournalCell
Volume92
Issue number6
DOIs
StatePublished - Mar 20 1998

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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