Structure of a complex between E. coli DNA topoisomerase I and single-stranded DNA

Kay Perry, Alfonso Mondragón*

*Corresponding author for this work

Research output: Contribution to journalArticle

32 Scopus citations

Abstract

In order to gain insights into the mechanism of ssDNA binding and recognition by Escherichia coli DNA topoisomerase I, the structure of the 67 kDa N-terminal fragment of topoisomerase I was solved in complex with ssDNA. The structure reveals a new conformational stage in the multistep catalytic cycle of type IA topoisomerases. In the structure, the ssDNA binding groove leading to the active site is occupied, but the active site is not fully formed. Large conformational changes are not seen; instead, a single helix parallel to the ssDNA binding groove shifts to clamp the ssDNA. The structure helps clarify the temporal sequence of conformational events, starting from an initial empty enzyme and proceeding to a ssDNA-occupied and catalytically competent active site.

Original languageEnglish (US)
Pages (from-to)1349-1358
Number of pages10
JournalStructure
Volume11
Issue number11
DOIs
StatePublished - Nov 2003

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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