Implications of Structures of Synaptic Tetramers of γδ Resolvase for the Mechanism of Recombination
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 determ...
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Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2006-07, Vol.103 (28), p.10642-10647 |
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Sprache: | eng |
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Zusammenfassung: | 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 fourhelix core, but differ in the relative orientations of its catalytic and DNA-binding domains. |
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ISSN: | 0027-8424 1091-6490 |
DOI: | 10.1073/pnas.0604062103 |