Abstract
The full three-dimensional structure determination of tomato bushy stunt virus has shown how its protein subunit can accommodate to different packing environments in the viral coat and how the size of the particle is nonetheless determined without ambiguity. Reversible, cooperative expansion of the virus at pH values above neutrality and in the absence of divalent cation requires further bonding alternatives for the subunit. We report here the structure of the expanded tomato bushy stunt virus particle, determined at 8 Å resolution by X-ray crystallography. Subunit conformational changes are localized, and folded domains are essentially invariant. The bonding properties of the subunit can account for controlled polymorphism of the assembly.
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Robinson, I., Harrison, S. Structure of the expanded state of tomato bushy stunt virus. Nature 297, 563–568 (1982). https://doi.org/10.1038/297563a0
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DOI: https://doi.org/10.1038/297563a0
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