Raman spectroscopic study on the conformation of a peptide fragment representing the DNA-binding domain of filamentous virus Pf3 coat protein.
Raman spectra have been measured of a nonapeptide which has an amino acid sequence identical to that of the C-terminal region of the major coat protein subunit of filamentous bacteriophage Pf3. The peptide shows a strong tendency to form a beta-sheet structure in aqueous solution. The beta-sheet formation is significantly promoted by complexation with single-stranded DNA but not with double-stranded DNA. It is suggested that the C-terminal region of the Pf3 coat protein binds to the single-stranded DNA genome in the virion with a beta-sheet conformation, in sharp contrast with the alpha-helical binding in other filamentous bacteriophages.
Miura
T
T
Pharmaceutical Institute, Tohoku University, Sendai, Japan.
Takeuchi
H
H
Harada
I
I
D000595:Amino Acid Sequence; D001435:Bacteriophages / Q000737:chemistry / Q000378:metabolism; D001665:Binding Sites; D002213:Capsid / Q000737:chemistry / Q000378:metabolism*; D004247:DNA / Q000378:metabolism*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D011487:Protein Conformation; D013059:Spectrum Analysis, Raman
D010446:Peptide Fragments; D004247:DNA