Three-dimensional structure of the Tn5 synaptic complex transposition intermediate

Science. 2000 Jul 7;289(5476):77-85. doi: 10.1126/science.289.5476.77.


Genomic evolution has been profoundly influenced by DNA transposition, a process whereby defined DNA segments move freely about the genome. Transposition is mediated by transposases, and similar events are catalyzed by retroviral integrases such as human immunodeficiency virus-1 (HIV-1) integrase. Understanding how these proteins interact with DNA is central to understanding the molecular basis of transposition. We report the three-dimensional structure of prokaryotic Tn5 transposase complexed with Tn5 transposon end DNA determined to 2.3 angstrom resolution. The molecular assembly is dimeric, where each double-stranded DNA molecule is bound by both protein subunits, orienting the transposon ends into the active sites. This structure provides a molecular framework for understanding many aspects of transposition, including the binding of transposon end DNA by one subunit and cleavage by a second, cleavage of two strands of DNA by a single active site via a hairpin intermediate, and strand transfer into target DNA.

Publication types

  • Comment
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Motifs
  • Binding Sites
  • Catalysis
  • Catalytic Domain
  • Crystallization
  • Crystallography, X-Ray
  • DNA / chemistry*
  • DNA / metabolism*
  • DNA Transposable Elements*
  • Dimerization
  • Manganese / metabolism
  • Mutation
  • Nucleic Acid Conformation
  • Plasmids
  • Protein Binding
  • Protein Conformation
  • Protein Folding
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Transposases / chemistry*
  • Transposases / genetics
  • Transposases / metabolism*


  • DNA Transposable Elements
  • Manganese
  • DNA
  • Transposases

Associated data

  • PDB/1F3I