Related Experiment Video
Updated: Jul 5, 2026

A G-quadruplex DNA-affinity Approach for Purification of Enzymatically Active G4 Resolvase1
Published on: March 18, 2017
Structure of a synaptic gammadelta resolvase tetramer covalently linked to two cleaved DNAs
Weikai Li1, Satwik Kamtekar, Yong Xiong
1Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA.
Abstract:
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.
Related Concept Videos
Fixing Double-strand Breaks
Homologous Recombination
Gene Conversion
Single-Strand DNA Binding Proteins
Restriction Enzymes
The host bacteria protect their own genomic DNA from these enzymes by methylating these sites. Some...
Nucleic Acid Structure
DNA Structure
DNA has a double-helix structure. The...

