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Published Online June 30, 2005
Science DOI: 10.1126/science.1112064

Research Articles

Submitted on March 9, 2005
Accepted on June 15, 2005

Structure of a Synaptic {gamma}{delta} Resolvase Tetramer Covalently Linked to Two Cleaved DNAs

Weikai Li 1, Satwik Kamtekar 1, Yong Xiong 2, Gary J. Sarkis 3, Nigel D. F. Grindley 1, Thomas A. Steitz 4*

1 Department of Molecular Biophysics and Biochemistry
2 Department of Molecular Biophysics and Biochemistry; Howard Hughes Medical Institute, Yale University, New Haven, Connecticut 06520, USA.
3 Department of Molecular Biophysics and Biochemistry; Present address: 454 Life Sciences, 20 Commercial Street, Branford, CT 06405, USA.
4 Department of Molecular Biophysics and Biochemistry; Department of Chemistry; Howard Hughes Medical Institute, Yale University, New Haven, Connecticut 06520, USA.

* To whom correspondence should be addressed.
Thomas A. Steitz , E-mail: eatherton{at}csb.yale.edu

The structure of a synaptic intermediate of the site-specific recombinase {gamma}{delta} resolvase covalently linked through Ser10 to two cleaved duplex DNAs has been determined at 3.4 Å resolution. This resolvase, activated for recombination by mutations, forms a tetramer whose structure is significantly changed from that of a pre-synaptic complex between dimeric resolvase and the cleavage site DNA. Since the two cleaved DNA duplexes that are to be recombined lie on opposite sides of the core tetramer, large movements of both protein and DNA are required to achieve strand exchange. The two dimers linked to the DNAs that are to be recombined are held together by a flat interface. This may allow a 180° rotation of one dimer relative to the other in order to reposition the DNA duplexes for strand exchange.


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Science. ISSN 0036-8075 (print), 1095-9203 (online)