Southern bean mosaic virus

Abad-Zapatero, C., et al. Structure of southern bean mosaic virus at 2.8 A resolution. Nature 286 33-39, 1980. 

Rossmann, M.G., et al. Subunit interactions in southern bean mosaic virus. J. Mol. Biol. 166 37-72, 1983. 

Coat protein, southern bean mosaic virus (Silva and Rossmann, 1985) X-ray 6 0.09 0.100... 

Tomato bushy stunt virus protein domains 2 and 3 Southern bean mosaic virus protein Concanavalin A... 

Serine proteases, see Trypsin, Chymotrypsin, Elastase, Strepto-myces griseus proteases A and B, or Subtilisin Southern bean mosaic virus protein (Abad-Zapatero et al., 1980) Jellyroll Greek key (3 barrel (Fig. 81)... 

Viral coat proteins, see Southern bean mosaic virus, Tobacco mosaic virus, or Tomato bushy stunt virus... 

Most of the EF-hand motifs have one water (—X). On the other hand, in Rhizopus chinensis aspartic proteinase (Suguna et al., 1987) there is one main-chain carbonyl oxygen bound to calcium and six water molecules to complete the pentagonal bipyramidal coordination. Calcium coordination has been measured in several viruses, such as Southern bean mosaic virus (Silva and Rossmann, 1985), satellite tobacco necrosis virus (Jones and Liljas, 1984), and tomato bushy stunt virus IV (Olson et al., 1983). 

Silva, A. M., and Rossmann, M. G. (1985). The refinement of southern bean mosaic virus in reciprocal space. Acta Crystallogr., Sect. B 41, 147—157. 

Southern bean mosaic virus (SBMV) particles are centrifuged at 12,590 rpm and the absorbance at 260 nm is measured along the settling direction as a function of time. The center of the absorption band varies with distance from the center of the rotor as follows ... 

The southern bean mosaic virus has an eight-stranded antiparallel (3-barrel structure closely similar to that of the major domain of the bushy stunt viruses but lacking the second hinged domain. The problem of quasi-equivalence is resolved by the presence of an N-terminal extension that binds onto a subunit across the quasi-six-fold axis to give a set of three subunits (labeled C in Fig. 7-19) that associate with true three-fold symmetry and another set (B) with a slightly different conformation fitting between them.68 92 The subunits A, which have a third conformation, fit together around the five-fold axis in true cyclic symmetry. 

Amino acid composition of southern bean mosaic virus. Contribs. Boyce Thompson Inst., 18, 371 (1956). With Beatrices. Magdoff and Diane Block Montie. 

SBMV. See Southern bean mosaic virus (SBMV)... 

Southern bean mosaic virus (SBMV), 204,226 x-ray crystallography of, 39 Spin-labeled influenza virus, electron spin resonance (ESR) and, 51 SPMV. See Satellite panicum mosaic virus (SPMV)... 

C-terminal interactions and, 267-268 X-ray analysis, of virus structure, 1, 3, 221 X-ray crystallography, 93-94, 221, 385-386 cryoelectron microscopy with, 54—56 of southern bean mosaic virus (SBMV), 39 of tomato bushy stunt virus (TBSV), 39 X-ray detectors, 40-41... 

Several plant viruses have been studied using X-ray crystallography and conventional X-ray sources. These are, in no particular order, TBSV (tomato bushy stunt virus), SBMV (southern bean mosaic virus) and STN V (satellite tobacco necrosis virus) - all spherical viruses - and TMV (tobacco mosaic virus) - a cylindrical virus. These virus crystals diffract relatively well and are reasonably stable to radiation. 

The tertiary fold of three of the rhinovirus proteins (VP1, VP2 and VP3) and their quaternary organisation within the HRV14 capsid are similar to the structures of the plant viruses TBSV (tomato bushy stunt virus) and SBMV (southern bean mosaic virus), agreeing to within approximately 3 A. In HRV14 VP4 is an internal structural protein in contact with VP1 and VP2. Protrusions on VP1, VP2 and VP3 together create a deep cleft or canyon on the viral surface which is 25 A deep and... 

Fig. 32. Typical experimental data ( + ) for an isometric protein-RNA plant virus, southern bean mosaic virus (SBMV) in its (a) compact and (b) swollen states [555]. For a given H20 buffer content, note the shift in the position of the subsidiary mimima to lower Q which accompanies the increase in the virus radius of about 10% in the swollen state. The continuous curve at each contrast is that calculated for a four-shell model of SBMV, and has been smeared to allow for neutron beam divergence and wavelength spread.

Zink, M., ScGrubmuller, H. (2009). Mechanical properties of the icosahedral shell of Southern bean mosaic virus A molecular dynamics study. Biophysical Journal, 96,1350. 

FIGURE 18 Structural arrangement of capsid proteins in southern bean mosaic virus, (a) The surface lattice describing the relationship between the three groups of 60 identical subunits, (b) The arrangement of protein subunits on the surface of the virus, (c) A ribbon representation of viral coat protein tor position A. 

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