Recognition of DNA sequences by the repressor of bacteriophage 434.
The structure of a complex between the DNA-binding domain of phage 434 repressor and a 14 base-pair synthetic DNA operator reveals the molecular interactions important for sequence-specific recognition. A set of contacts with DNA backbone, notably involving hydrogen bonds between peptide-NH groups and DNA phosphates, position the repressor and fix the DNA configuration. Direct interactions between amino acid side chains and DNA bases involve nonpolar van der Waals contacts as well as hydrogen bonds. The structures of the repressor domain and of the 434 cro protein are extremely similar. There appear to be no major conformational changes in the proteins when they bind to DNA.
Harrison
S C
SC
Department of Biochemistry and Molecular Biology, Harvard University, Cambridge, MA.
Anderson
J E
JE
Koudelka
G B
GB
Mondragon
A
A
Subbiah
S
S
Wharton
R P
RP
Wolberger
C
C
Ptashne
M
M
D001435:Bacteriophages / Q000235:genetics*; D001665:Binding Sites; D003461:Crystallography; D004279:DNA, Viral / Q000378:metabolism*; D008958:Models, Molecular; D009711:Nucleotides / Q000378:metabolism; D009876:Operon; D012097:Repressor Proteins / Q000502:physiology*; D014157:Transcription Factors / Q000502:physiology*
D004279:DNA, Viral; D009711:Nucleotides; D012097:Repressor Proteins; D014157:Transcription Factors