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1zr2

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(New page: 200px<br /><applet load="1zr2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zr2, resolution 3.90&Aring;" /> '''Structure of a Synap...)
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Revision as of 05:29, 21 November 2007


1zr2, resolution 3.90Å

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Structure of a Synaptic gamma-delta Resolvase Tetramer Covalently Linked to two Cleaved DNAs

Overview

The structure of a synaptic intermediate of the site-specific recombinase, gammadelta resolvase covalently linked through Ser10 to two cleaved duplex, DNAs has been determined at 3.4 angstrom resolution. This resolvase, activated for recombination by mutations, forms a tetramer whose structure, is substantially changed from that of a presynaptic complex between, dimeric resolvase and the cleavage site DNA. Because 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, degrees rotation of one dimer relative to the other in order to reposition, the DNA duplexes for strand exchange.

About this Structure

1ZR2 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structure of a synaptic gammadelta resolvase tetramer covalently linked to two cleaved DNAs., Li W, Kamtekar S, Xiong Y, Sarkis GJ, Grindley ND, Steitz TA, Science. 2005 Aug 19;309(5738):1210-5. Epub 2005 Jun 30. PMID:15994378

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