Structure of the stacked disk aggregate of tobacco mosaic virus protein

Biophysical Journal
R Díaz-Avalos, D L Caspar

Abstract

The coat protein of tobacco mosaic virus is known to form three different classes of aggregate, depending on environmental conditions, namely helical, disk, and A-protein. Among the disk aggregates, there are four-layer, six-layer, and long stacks, which can be obtained by varying the ionic strength and temperature conditions during the association process. The four-layer aggregate has been crystallized, and its structure solved to atomic resolution. The stacked disk aggregate had been presumed to be built of a polar two-layer disk related to the crystalline A and B rings. A study using monoclonal antibodies specific to the bottom surface of TMV protein demonstrated that the stacked disk aggregate is bipolar, and suggested that the repeating two-layer unit might be similar to the dihedrally symmetrical A-ring pair in the disk crystal. In this paper we present a three-dimensional reconstruction of the stacked disk aggregate obtained by electron microscopy of ice-embedded samples. After modeling of the structure, we found the ring pairs to have the same quaternary structure as the A-ring pair of the four-layer aggregate. The resolution achieved in the image processing of the electron micrographs is on the order of 9 A in the meri...Continue Reading

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Citations

Apr 23, 1999·Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences·A Klug
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Jan 7, 2003·Physical Review. E, Statistical, Nonlinear, and Soft Matter Physics·T G Mason
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