Three-dimensional structure of the 67K N-terminal fragment of E. coli DNA topoisomerase I

Christopher D. Lima, James C. Wang, Alfonso Mondragon*

*Corresponding author for this work

Research output: Contribution to journalArticle

244 Scopus citations

Abstract

The three-dimensional structure of the 67K amino-terminal fragment of Escherichia coli DNA topoisomerase I has been determined to 2.2 Å resolution. The polypeptide folds in an unusual way to give four distinct domains enclosing a hole large enough to accommodate a double-stranded DNA. The active-site tyrosyl residue, which is involved in the transient breakage of a DNA strand and the formation of a covalent enzyme-DNA intermediate, is present at the interface of two domains. The structure suggests a plausible mechanism by which E. coli DNA topoisomerase I and other members of the same DNA topoisomerase subfamily could catalyse the passage of one DNA strand through a transient break in another strand.

Original languageEnglish (US)
Pages (from-to)138-146
Number of pages9
JournalNature
Volume367
Issue number6459
DOIs
StatePublished - Jan 1 1994

ASJC Scopus subject areas

  • General

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