Structure of the stacked disk aggregate of tobacco mosaic virus protein.

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 meridional direction and 12 A 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 approximately 53 A when fully hydrated, can shrink to approximately 43 A in the dry state.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Díaz-Avalos R,Caspar DL

doi

10.1016/S0006-3495(98)77818-X

subject

Has Abstract

pub_date

1998-01-01 00:00:00

pages

595-603

issue

1

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(98)77818-X

journal_volume

74

pub_type

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