The wac gene product of bacteriophage T4 contains coiled-coil structural patterns.
The bacteriophage T4 late gene wac (whisker antigen control) encodes the protein which forms the fibrous structure on the neck of the virion called whiskers. Amino acid sequence analysis of wac gene product, as deduced from the nucleotide sequence, indicate ten alpha-helical domains (19-40 residues long) with coiled-coil structural patterns. These regions comprise about 70% of the entire 486 amino acid sequence. The alpha-helices are separated by short stretches of polypeptide chain which are similar to the loop regions of the globular protein sequences. We propose a structural model for the dimer of wac gene product molecule, that we call fibritin in which two polypeptide chains associate in a parallel fashion and form a segmented alpha-helical coiled-coil rod similar to epidermal keratins.
Sobolev
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BN
Department of Basic Virology, D.I. Ivanovsky Institute of Virology, USSR Academy of Medical Sciences, Moscow.
Mesyanzhinov
V V
VV
D000595:Amino Acid Sequence; D005583:Fourier Analysis; D005814:Genes, Viral; D008969:Molecular Sequence Data; D011487:Protein Conformation; D013604:T-Phages / Q000235:genetics*; D014764:Viral Proteins / Q000737:chemistry* / Q000235:genetics
D014764:Viral Proteins; C057839:fibritin protein, Enterobacteria phage T4