1smv
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(New page: 200px<br /><applet load="1smv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1smv, resolution 3.Å" /> '''PRIMARY STRUCTURE OF S...)
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Revision as of 22:40, 24 November 2007
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PRIMARY STRUCTURE OF SESBANIA MOSAIC VIRUS COAT PROTEIN: ITS IMPLICATIONS TO THE ASSEMBLY AND ARCHITECTURE OF THE VIRUS
Overview
BACKGROUND: Sobemoviruses are a group of RNA plant viruses that have a, narrow host range. They are characterized in vitro by their stability, high thermal inactivation point and longevity. The three-dimensional, structure of only one virus belonging to this group, southern bean mosaic, virus (SBMV), is known. Structural studies on sesbania mosaic virus (SMV), which is closely related to SBMV, will provide details of the molecular, interactions that are likely to be important in the stability and assembly, of sobemoviruses. RESULTS: We have determined the three-dimensional, structure of SMV at 3 A resolution. The polypeptide fold and quaternary, organization are very similar to those of SBMV. The capsid consists of, sixty icosahedral asymmetric units, each comprising three copies of a, chemically identical coat protein subunit, which are designated as A, B, and C and are in structurally different environments. Four cation-binding, sites have been located in the icosahedral asymmetric unit. Of these, the, site at the quasi-threefold axis is not found in SBMV. Structural, differences are observed in loops and regions close to this cation-binding, site. Preliminary studies on ethylene diamine tetra acetic acid (EDTA), treated crystals suggest asymmetry in removal of the quasi-equivalent, cations at the AB, BC, and AC subunit interfaces. CONCLUSIONS: Despite the, overall similarity between SMV and SBMV in the nature of the polypeptide, fold, these viruses show a number of differences in intermolecular, interactions. The polar interactions at the quasi-threefold axis are, substantially less in SMV and positively charged residues on the, RNA-facing side of the protein and in the N-terminal arm are not, particularly well conserved. This suggests that protein-RNA interactions, are likely to be different between the two viruses.
About this Structure
1SMV is a Single protein structure of sequence from Sesbania mosaic virus with CA as ligand. Full crystallographic information is available from OCA.
Reference
Structure of sesbania mosaic virus at 3 A resolution., Bhuvaneshwari M, Subramanya HS, Gopinath K, Savithri HS, Nayudu MV, Murthy MR, Structure. 1995 Oct 15;3(10):1021-30. PMID:8589997
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