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• W2093623967 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 Å in the meridional direction and 12 Å in the equatorial. The identification of the structure of the stacked disk with the A-ring pair of the disk crystal provides an explanation of the observation that the axial periodicity of the disk pair, which is ∼53 Å when fully hydrated, can shrink to ∼43 Å in the dry state." @default.
• W2093623967 created "2016-06-24" @default.
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• W2093623967 date "1998-01-01" @default.
• W2093623967 modified "2023-10-16" @default.
• W2093623967 title "Structure of the Stacked Disk Aggregate of Tobacco Mosaic Virus Protein" @default.
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• W2093623967 doi "https://doi.org/10.1016/s0006-3495(98)77818-x" @default.
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