title: Structure of phage phi 29 connector protein assembled in vivo.
abstract: The protein p10 that forms the connector of phage phi 29, has been produced in Escherichia coli harboring a plasmid that carried the gene coding for this protein. The connector protein is assembled in a 13.4-S oligomer that has an apparent molecular weight of 460,000, suggesting that it is a dodecamer. The purified oligomers have been studied by electron microscopy of the isolated particles as well as by image-processing techniques (Fourier and rotational filtering) of artificially induced two-dimensional aggregates. The results show that the purified p10 is assembled in a circular structure with a hole in its center and 12 morphological units in the periphery. Both the morphology and the dimensions of this p10 oligomer are very similar to those of the upper neck collar extracted from phi 29 viral particles. The results strongly suggest the close relationship between the p10 oligomers assembled in E. coli and the ones produced in phi 29 infected Bacillis subtilis.
mesh_terms: D001412:Bacillus subtilis; D001435:Bacteriophages / Q000032:analysis*; D002499:Centrifugation, Density Gradient; D004926:Escherichia coli / Q000378:metabolism; D005583:Fourier Analysis; D046911:Macromolecular Substances; D008854:Microscopy, Electron; D008970:Molecular Weight; D010957:Plasmids; D011487:Protein Conformation; D014764:Viral Proteins
chemical_list: D046911:Macromolecular Substances; D014764:Viral Proteins