Implications of structures of synaptic tetramers of γδ resolvase for the mechanism of recombination

Satwik Kamtekar, Roger S. Ho, Melanie J. Cocco, Weikai Li, Sandra V.C.T. Wenwieser, Martin R. Boocock, Nigel D.F. Grindley, Thomas A. Steitz

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The structures of two mutants of the site-specific recombinase, γδ resolvase, that form activated tetramers have been determined. One, at 3.5-Å resolution, forms a synaptic intermediate of resolvase that is covalently linked to two cleaved DNAs, whereas the other is of an unliganded structure determined at 2.1-Å resolution. Comparisons of the four known tetrameric resolvase structures show that the subunits interact through the formation of a common core of four helices. The N-terminal halves of these helices superimpose well on each other, whereas the orientations of their C termini are more variable. The catalytic domains of resolvase in the unliganded structure are arranged asymmetrically, demonstrating that their positions can move substantially while preserving the four-helix core that forms the tetramer. These results suggest that the precleavage synaptic tetramer of γδ resolvase, whose structure is not known, may be formed by a similar four-helix core, but differ in the relative orientations of its catalytic and DNA-binding domains.

Original languageEnglish
Pages (from-to)10642-10647
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number28
StatePublished - Jul 11 2006


  • Cleaved complex
  • Crystallography
  • Hyperactive mutant
  • Serine recombinase
  • Site-specific recombination


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