volume 103, issue 28, P10642-10647 2006
DOI: 10.1073/pnas.0604062103
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Abstract: The structures of two mutants of the site-specific recombinase, ␥␦ 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…

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