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Protein-RNA interactions in tobacco mosaic virus

Journal Article · · Biophys. J.; (United States)
Tobacco mosaic virus (TMV) is a rod-shaped virus, 3000 A long and 180 A in diameter. It has helical symmetry, with 49 coat protein subunits in three turns. A single strand of RNA follows the basic helix at 40 A radius, with three nucleotides bound to each protein subunit. Using x-ray diffraction from oriented gels and a technique analogous to crystallographic isomorphous replacement Stubbs et al. solved the structure of the intact virus to a resolution of 4 A. The electron density map they produced has been improved by applying an envelope function to the map, back-transforming, and applying the resulting phases to the observed data. This is commonly used in protein crystallography, and is a much more powerful constraint in fiber diffraction. The interpretation of the map has been improved by consideration of maps of the protein helix, which is structurally almost identical to the virus, except for the absence of the RNA. The RNA model has been improved by computer model-building techniques as described below.
Research Organization:
Brandeis Univ., Waltham, MA
OSTI ID:
6796130
Journal Information:
Biophys. J.; (United States), Journal Name: Biophys. J.; (United States) Vol. 32:1; ISSN BIOJA
Country of Publication:
United States
Language:
English