Structure of the capsid of Kilham rat virus from small-angle neutron scattering.
The structure of empty capsids of Kilham rat virus, an autonomous parvovirus with icosahedral symmetry, was investigated by small-angle neutron scattering. From the forward scatter, the molecular weight was determined to be 4.0 X 10(6), and from the Guinier region, the radius of gyration was found to be 105 A in D2O and 104 A in H2O. On the basis of the capsid molecular weight and the molecular weights and relative abundances of the capsid proteins, we propose that the capsid has a triangulation number of 1. Extended scattering curves and mathematical modeling revealed that the capsid consists of two shells of protein, the inner shell extending from 58 to 91 A in D2O and from 50 to 91 A in H2O and containing 11% of the capsid scattering mass, and the outer shell extending to 121 A in H2O and D2O. The inner shell appears to have a higher content of basic amino acids than the outer shell, based on its lower scattering density in D2O than in H2O. We propose that all three capsid proteins contribute to the inner shell and that this basic region serves DNA binding and partial charge neutralization functions.
D000596:Amino Acids / Q000032:analysis; D002213:Capsid / Q000648:ultrastructure*; D008954:Models, Biological; D008970:Molecular Weight; D009502:Neutrons; D010321:Parvoviridae / Q000648:ultrastructure*; D011487:Protein Conformation; D012542:Scattering, Radiation
D000596:Amino Acids