title: Structure of the amino-terminal domain of phage 434 repressor at 2.0 A resolution.
abstract: The crystal structure of the amino-terminal domain of phage 434 repressor has been solved using molecular replacement methods and refined to an R-factor of 19.3% against data to 2.0 A resolution. The protein comprises five short alpha-helices. Two of these form a helix-turn-helix motif, very similar to those found in related proteins. The protein is remarkably similar to the Cro protein from the same phage.
authors.affiliation: Department of Biochemistry and Molecular Biology, Harvard University, Cambridge, MA.
authors.forename: A
authors.initials: A
authors.lastname: Mondragón
authors.forename: S
authors.initials: S
authors.lastname: Subbiah
authors.forename: S C
authors.initials: SC
authors.lastname: Almo
authors.forename: M
authors.initials: M
authors.lastname: Drottar
authors.forename: S C
authors.initials: SC
authors.lastname: Harrison
mesh_terms: D000595:Amino Acid Sequence; D001435:Bacteriophages / Q000235:genetics*; D004268:DNA-Binding Proteins / Q000235:genetics; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D012097:Repressor Proteins / Q000235:genetics*; D014157:Transcription Factors / Q000235:genetics*; D014764:Viral Proteins / Q000235:genetics*; D054334:Viral Regulatory and Accessory Proteins; D014961:X-Ray Diffraction
chemical_list: D004268:DNA-Binding Proteins; D012097:Repressor Proteins; D014157:Transcription Factors; D014764:Viral Proteins; D054334:Viral Regulatory and Accessory Proteins; C016649:phage repressor proteins