Structures of the helical aggregates of tobacco mosaic virus protein

Mandelkow, Eckhard; Stubbs, Gerald J.; Warren , Stephen

doi:10.1016/0022-2836(81)90248-5 Get

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Structures of the helical aggregates of tobacco mosaic virus protein

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Mandelkow, Eckhard
Arbeitsgruppe Zytoskelett, Max Planck Institute for Medical Research, Max Planck Society;
Eckhard Mandelkow, Emeriti, Max Planck Institute for Metabolism Research, Managing Director: Jens Brüning, Max Planck Society;
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Mandelkow, E., Stubbs, G. J., & Warren, S. (1981). Structures of the helical aggregates of tobacco mosaic virus protein. Journal of Molecular Biology (London), 152(2), 375-382. doi:10.1016/0022-2836(81)90248-5 Get.

Cite as: https://hdl.handle.net/21.11116/0000-0004-E7C5-9

Abstract

Tobacco mosaic virus coat protein forms two helical aggregates, with and subunits per turn. Both have been studied and compared with the intact virus by recording X-ray diffraction from oriented gels and calculating difference Fourier maps. The protein forms have structures very similar to each other and to the protein part of the virus, even in the low radius region, which has a very different structure in the crystalline disk form of the protein. The RNA is replaced in the helical protein forms by at least one bound anion. The difference between the protein forms may possibly be related to the conformation of one or more of the arginine groups that bind RNA in the intact virus.