The carboxyl-terminal domain of gamma delta resolvase binds to each half of the three resolvase binding sites that constitute the recombination site, res. Ethylation inhibition experiments show that the phosphate contacts made by the C-terminal DNA binding domain are similar to those made by intact resolvase, with the exception of a single phosphate at the inside end of each contact region which is contacted solely by the intact resolvase. The DNA binding domain makes essentially identical contacts to all 6 half sites, whereas the intact resolvase makes slightly different contacts to each binding site. Despite its small size, only 43 amino acid residues, the resolvase C-terminal domain interacts with an unusually large segment of DNA. Phosp...
Replication Factor C (RFC) is a five-subunit protein complex required for eukaryotic DNA replication...
AbstractBackground: The inverted repeat is a common feature of protein-binding sites in DNA. The two...
To characterize the residues that participate in the catalysis of DNA cleavage and rejoining by the ...
The carboxyl-terminal domain of gamma delta resolvase binds to each half of the three resolvase bind...
The carboxyl-terminal domain of gamma delta resolvase binds to each half of the three resolvase bind...
The DNA binding domain of γδ-resolvase, residues 141-183, is thought to bind DNA by a helix-turn-hel...
During site-specific recombination by the gamma delta resolvase, four DNA strands are broken, exchan...
The resolvase encoded by the transposon gamma delta mediates a site-specific recombination between t...
The crystal structure of the catalytic domain of the site-specific recombination enzyme gamma delta ...
AbstractThe structure of γδ resolvase complexed with a 34 bp substrate DNA has been determined at 3....
gamma delta resolvase, a transposon-encoded protein active in site-specific recombination, induces a...
We have been studying the crystal structure of three proteins that interact with DNA: the E. coli ca...
During site-specific recombination by the γδ resolvase, four DNA strands are broken, exchanged, and ...
Incorporation of the DNA-cleaving moiety EDTA•Fe at discrete amino acid residues along a DNA-binding...
Resolvases from Tnd-like transposons catalyse site-specific recombination at res sites. Each res sit...
Replication Factor C (RFC) is a five-subunit protein complex required for eukaryotic DNA replication...
AbstractBackground: The inverted repeat is a common feature of protein-binding sites in DNA. The two...
To characterize the residues that participate in the catalysis of DNA cleavage and rejoining by the ...
The carboxyl-terminal domain of gamma delta resolvase binds to each half of the three resolvase bind...
The carboxyl-terminal domain of gamma delta resolvase binds to each half of the three resolvase bind...
The DNA binding domain of γδ-resolvase, residues 141-183, is thought to bind DNA by a helix-turn-hel...
During site-specific recombination by the gamma delta resolvase, four DNA strands are broken, exchan...
The resolvase encoded by the transposon gamma delta mediates a site-specific recombination between t...
The crystal structure of the catalytic domain of the site-specific recombination enzyme gamma delta ...
AbstractThe structure of γδ resolvase complexed with a 34 bp substrate DNA has been determined at 3....
gamma delta resolvase, a transposon-encoded protein active in site-specific recombination, induces a...
We have been studying the crystal structure of three proteins that interact with DNA: the E. coli ca...
During site-specific recombination by the γδ resolvase, four DNA strands are broken, exchanged, and ...
Incorporation of the DNA-cleaving moiety EDTA•Fe at discrete amino acid residues along a DNA-binding...
Resolvases from Tnd-like transposons catalyse site-specific recombination at res sites. Each res sit...
Replication Factor C (RFC) is a five-subunit protein complex required for eukaryotic DNA replication...
AbstractBackground: The inverted repeat is a common feature of protein-binding sites in DNA. The two...
To characterize the residues that participate in the catalysis of DNA cleavage and rejoining by the ...