1zr4
From Proteopedia
Structure of a Synaptic gamma-delta Resolvase Tetramer Covalently linked to two Cleaved DNAs
Structural highlights
FunctionTNR1_ECOLI This protein catalyzes the site-specific recombination of the transposon and also regulates its frequency of transposition. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. Loading citation details.. Citations No citations found See AlsoReferences
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Categories: Escherichia coli | Large Structures | Grindley ND | Kamtekar S | Li W | Sarkis GJ | Steitz TA | Xiong Y
