Structure of Sesbania mosaic virus at 3 angstrom resolution

Murthy, MRN and Bhuvaneswari, M and Subramanya, HS and Gopinath, K and Savithri, HS (1997) Structure of Sesbania mosaic virus at 3 angstrom resolution. In: Biophysical Chemistry, 68 (1-3). pp. 33-42.

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Abstract

Sesbania mosaic virus (SMV) is an isometric, ss-RNA plant virus found infecting Sesbania grandiflora plants in fields near Tirupathi, South India. The virus particles, which sediment at 116 S at pH 5.5, swell upon treatment with EDTA at pH 7.5 resulting in the reduction of the sedimentation coefficient to 108 S. SMV coat protein amino acid sequence was determined and found to have approximately 60% amino acid sequence identity with that of southern bean mosaic virus (SBMV). The amino terminal 60 residue segment, which contains a number of positively charged residues, is less well conserved between SMV and SBMV when compared to the rest of the sequence. The 3D structure of SMV was determined at 3.0 Å resolution by molecular replacement techniques using SBMV structure as the initial phasing model. The icosahedral asymmetric unit was found to contain four calcium ions occurring in inter subunit interfaces and three protein subunits, designated A, B and C. The conformation of the C subunit appears to be different from those of A and B in several segments of the polypeptide. These observations coupled with structural studies on SMV partially depleted of calcium suggest a plausible mechanisms for the initiation of the disassembly of the virus capsid.

Item Type:	Journal Article
Publication:	Biophysical Chemistry
Publisher:	Elsevier Sceince
Additional Information:	Copyright for this article belongs to Elsevier Sceince.
Keywords:	Sesbania mosaic virus; Protein structure; X-Ray diffraction; Disassembly
Department/Centre:	Division of Biological Sciences > Molecular Biophysics Unit Division of Biological Sciences > Biochemistry
Date Deposited:	18 Jan 2010 08:58
Last Modified:	19 Sep 2010 05:51
URI:	http://eprints.iisc.ac.in/id/eprint/24711

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