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Journal Article

A new helical aggregate of Tobacco Mosaic Virus Protein

MPS-Authors
/persons/resource/persons94203

Mandelkow,  Eckhard
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;
Arbeitsgruppe Zytoskelett, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons93463

Holmes,  Kenneth C.
Protein Cristallography XDS, Max Planck Institute for Medical Research, Max Planck Society;
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;
Muscle Research, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons123645

Gallwitz,  Ute
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

External Resource

https://www.sciencedirect.com/science/article/pii/S0022283676800538/pdf?md5=58ad0bc2c3dc1e8a93ac4ea1f1fc699a&pid=1-s2.0-S0022283676800538-main.pdf
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https://doi.org/10.1016/S0022-2836(76)80053-8
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Citation

Mandelkow, E., Holmes, K. C., & Gallwitz, U. (1976). A new helical aggregate of Tobacco Mosaic Virus Protein. Journal of Molecular Biology (London), 102(2), 265-285. doi:10.1016/S0022-2836(76)80053-8.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0019-B136-3
Abstract
Tobacco mosaic virus coat protein has been repolymerized in the absence of RNA and investigated by X-ray analysis. The rods obtained can be classified in two different helical surface lattices (class A and B), having nearly 16 1/3 and 17 1/3 subunits per turn, respectively, with only small differences in polypeptide chain folding. The structure of the protein rod in helix class A is almost identical with that in intact tobacco mosaic virus, while in the absence of the RNA the class B surface lattice is predominant.