Primary structure and sidechain interactions of PFL filamentous bacterial virus coat protein

Molecular models and structural comparisons of native and mutant class I filamentous bacteriophages

“…Direct interpretation of the strong intensity distribution on low-resolution diffraction patterns, followed by molecular model-building, energy refinement, and comparison of calculated Fourier transforms with observed diffraction data, gave the orientation of the a-helix within the surface lattice of the virion and indicated a common subunit shape and a common molecular architecture for all strains (Marvin et al, 1974a, b;Marvin & Wachtel, 1975, 1976. The proposal of a common architecture was supported by the discovery that, despite differences in detail, both class I and class II g8p sequences have the same characteristic distribution of aminoacid residues, with several acidic residues near the N terminus, a 19-residue apolar domain near the middle and a cluster of basic residues near the C terminus (Nakashima et al, 1975). The subunits in the model are gently curved a-helix rods in an overlapping interdigitated helical array.…”

Subtilisin removes the surface layer of the phage fd coat

“…The primary structure of the mature polypeptide chain (in fd 50 amino acids with a molecular mass of 5340 Da) displays three different domains (Fig. 1); acidic amino acids, clustered at the N-terminal part on the phage surface; a central, hydrophobic domain, assumed to be responsible for protein/protein-interactions in the phage coat and for its transmembrane function in the host cell (Nakashima et al, 1975;Zimmermann et al, 1986); a basic region at the Cterminus involving four lysing residue (Makowski, 1984). In the phage coat g8p adopts a quasi 100% helical secondary structure arranged on two layers.…”

Conformational studies of hepatitis B surface antigen (HBsAg) by amino acid analysis.

“…Thus it seems probable that HBsAg might have true a-helical structure in spite of its higher content of non-a-helical amino acid residues. The same kind of observation was recently made with fd phage which contained almost 100% a-helical structure (Nakashima et al 1975). …”