Protein-DNA conformational changes in the crystal structure of a lambda Cro-operator complex.
AUTOR(ES)
Brennan, R G
RESUMO
The structure of a complex of bacteriophage lambda Cro protein with a 17-base-pair operator has been determined at 3.9-A resolution. Isomorphous derivatives obtained by the synthesis of site-specific iodinated DNA oligomers were of critical importance in solving the structure. The crystal structure contains three independent Cro-operator complexes that have very similar, although not necessarily identical, conformations. In the complex, the protein dimer undergoes a large conformational change relative to the crystal structure of the free protein. One monomer rotates by about 40 degrees relative to the other, this being accomplished primarily by a twisting of the two beta-sheet strands that connect one monomer with the other. In the complex, the DNA is bent by about 40 degrees into the shape of a boomerang but maintains essentially Watson-Crick B-form. In contrast to other known protein-DNA complexes, the DNA is not stacked end-to-end. The structure confirms the general features of the model previously proposed for the interaction of Cro with DNA.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=54913Documentos Relacionados
- Thermodynamics of Cro protein-DNA interactions.
- Cold denaturation of a repressor-operator complex: the role of entropy in protein-DNA recognition.
- Immunodepletion EMSA: a novel method to identify proteins in a protein-DNA complex.
- Crystal structure of the CENP-B protein–DNA complex: the DNA-binding domains of CENP-B induce kinks in the CENP-B box DNA
- Synthesis of isotope labeled oligonucleotides and their use in an NMR study of a protein-DNA complex.