Abstract
Two structural classes of filamentous bacterial viruses have been identified on the basis of their X-ray diffraction patterns. The class I structure1 is found for the fd, If1 and IKe strains, while the class II structure2 is found for the Pf1 and Xf strains. The two classes differ in the number of protein subunits per turn in the virus helix (4.5 units per turn for class I and 4.4 for class II, with ∼15 Å pitch), and in the fact that a periodic perturbation of the structure is observed for class I but not for class II. The major coat protein, which comprises about 99% of the virus coat, is largely α-helical3,4 with a molecular weight of about 5,000 for all strains investigated2. The sequence of the fd coat protein4,5 is known. It is 50 residues long, with an acidic N-terminal region, a hydrophobic middle region and a basic C-terminal region. To facilitate the detailed analysis of the class II structure, and to investigate the possibility that the structural differences between class I and class II arise from differences in the coat protein, we have determined the sequence of Pf1 coat protein. This is the first system for which a molecular model of a structural protein has been described in sufficient detail to permit study of the bonding specificity between proteins. Since the α helix is a universal structure, study of the interactions between α helices can be of central importance in many unrelated systems. We have found that α helices are arranged in the virion so that hydrophobic sidechains on each protein subunit can fit into the space between sidechains on neighbouring subunits.
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NAKASHIMA, Y., WISEMAN, R., KONIGSBERG, W. et al. Primary structure and sidechain interactions of PFL filamentous bacterial virus coat protein. Nature 253, 68–71 (1975). https://doi.org/10.1038/253068a0
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DOI: https://doi.org/10.1038/253068a0
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