Structure of the amino-terminal domain of phage 434 repressor at 2.0 A resolution.
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.
Mondragón
A
A
Department of Biochemistry and Molecular Biology, Harvard University, Cambridge, MA.
Subbiah
S
S
Almo
S C
SC
Drottar
M
M
Harrison
S C
SC
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
D004268:DNA-Binding Proteins; D012097:Repressor Proteins; D014157:Transcription Factors; D014764:Viral Proteins; D054334:Viral Regulatory and Accessory Proteins; C016649:phage repressor proteins