title: Structure of a phage 434 Cro/DNA complex.
abstract: Comparison of the crystal structure of a complex of the phage 434 Cro protein and a synthetic DNA operator with the complex of the same operator and the 434 repressor DNA-binding domain shows different DNA conformations in the two structures. Binding of the protein determines the precise conformation of the DNA in each case.
authors.affiliation: Department of Biochemistry and Molecular Biology, Harvard University, Cambridge, Massachusetts.
authors.forename: C
authors.initials: C
authors.lastname: Wolberger
authors.forename: Y C
authors.initials: YC
authors.lastname: Dong
authors.forename: M
authors.initials: M
authors.lastname: Ptashne
authors.forename: S C
authors.initials: SC
authors.lastname: Harrison
mesh_terms: D001435:Bacteriophages / Q000235:genetics*; D001482:Base Composition; D001483:Base Sequence; D001665:Binding Sites; D004279:DNA, Viral / Q000378:metabolism*; D004268:DNA-Binding Proteins; D046911:Macromolecular Substances; D015394:Molecular Structure; D009690:Nucleic Acid Conformation; D009875:Operator Regions, Genetic; D011487:Protein Conformation; D012097:Repressor Proteins / Q000378:metabolism*; D014157:Transcription Factors / Q000378:metabolism*; D014764:Viral Proteins; D054334:Viral Regulatory and Accessory Proteins; D014961:X-Ray Diffraction
chemical_list: D004279:DNA, Viral; D004268:DNA-Binding Proteins; D046911:Macromolecular Substances; D012097:Repressor Proteins; D014157:Transcription Factors; D014764:Viral Proteins; D054334:Viral Regulatory and Accessory Proteins; C016649:phage repressor proteins