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Structure of southern bean mosaic virus at 2.8 Å resolution Celerino Abad-Zapatero, Sherin S. Abdel-Meguid, John E. Johnson, Andrew G. W. Leslie*, Ivan Rayment†, Michael G. Rossmann, Dietrich Suck‡ & Tomitake Tsukihara§
Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907 Present addresses: * Biophysics Section, Blackett Laboratory, Imperial College of Science and Technology, Prince Consort Road, London SW7 2BZ, UK; † Structural Biology Laboratory, Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, Massachusetts 02154; ‡ European Molecular Biology Laboratory, Postfach 10 22 09, 69 Heidelberg 1, FRG; § Department of Chemistry, Faculty of Engineering, Tottori University, Koyama-cho, Tottori 680, Japan.
X-ray diffraction studies reveal that the polypeptide chain of the southern bean mosaic virus protein subunit has a fold closely similar to the shell domain of tomato bushy stunt virus. The protruding domain of tomato bushy stunt virus is absent in southern bean mosaic virus. The tertiary structure observed in these viruses may be particularly suitable f or the formation of the protein coat in small, spherical, RNA-containing, plant viruses.
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