Structure of a synaptic γδ resolvase tetramer covalently linked to two cleaved DNAS

Weikai Li; Satwik Kamtekar; Yong Xiong; Gary J. Sarkis; Nigel D.F. Grindley; Thomas A. Steitz

Structure of a synaptic γδ resolvase tetramer covalently linked to two cleaved DNAS

Weikai Li, Satwik Kamtekar, Yong Xiong, Gary J. Sarkis, Nigel D.F. Grindley, Thomas A. Steitz

Research output: Chapter in Book/Report/Conference proceeding › Chapter › peer-review

Abstract

The structure of a synaptic intermediate of the site-specific recombinase γδ 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° rotation of one dimer relative to the other in order to reposition the DNA duplexes for strand exchange.

Original language	English
Title of host publication	Structural Insights into Gene Expression and Protein Synthesis
Publisher	World Scientific Publishing Co.
Pages	447-452
Number of pages	6
ISBN (Electronic)	9789811215865
ISBN (Print)	9789811215858
State	Published - Jan 1 2020

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abstract = "The structure of a synaptic intermediate of the site-specific recombinase γδ 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° rotation of one dimer relative to the other in order to reposition the DNA duplexes for strand exchange.",

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T1 - Structure of a synaptic γδ resolvase tetramer covalently linked to two cleaved DNAS

AU - Li, Weikai

AU - Kamtekar, Satwik

AU - Xiong, Yong

AU - Sarkis, Gary J.

AU - Grindley, Nigel D.F.

AU - Steitz, Thomas A.

PY - 2020/1/1

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N2 - The structure of a synaptic intermediate of the site-specific recombinase γδ 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° rotation of one dimer relative to the other in order to reposition the DNA duplexes for strand exchange.

AB - The structure of a synaptic intermediate of the site-specific recombinase γδ 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° rotation of one dimer relative to the other in order to reposition the DNA duplexes for strand exchange.

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BT - Structural Insights into Gene Expression and Protein Synthesis

PB - World Scientific Publishing Co.

ER -

Structure of a synaptic γδ resolvase tetramer covalently linked to two cleaved DNAS

Abstract

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