Literature DB >> 15713465

Crystallographic structure of the T=1 particle of brome mosaic virus.

Steven B Larson1, Robert W Lucas, Alexander McPherson.   

Abstract

T=1 icosahedral particles of amino terminally truncated brome mosaic virus (BMV) protein were created by treatment of the wild-type T=3 virus with 1M CaCl2 and crystallized from sodium malonate. Diffraction data were collected from frozen crystals to beyond 2.9 A resolution and the structure determined by molecular replacement and phase extension. The particles are composed of pentameric capsomeres from the wild-type virions which have reoriented with respect to the original particle pentameric axes by rotations of 37 degrees , and formed tenuous interactions with one another, principally through conformationally altered C-terminal polypeptides. Otherwise, the pentamers are virtually superimposable upon those of the original T=3 BMV particles. The T=1 particles, in the crystals, are not perfect icosahedra, but deviate slightly from exact symmetry, possibly due to packing interactions. This suggests that the T=1 particles are deformable, which is consistent with the loose arrangement of pentamers and latticework of holes that penetrate the surface. Atomic force microscopy showed that the T=3 to T=1 transition could occur by shedding of hexameric capsomeres and restructuring of remaining pentamers accompanied by direct condensation. Knowledge of the structures of the BMV wild-type and T=1 particles now permit us to propose a tentative model for that process. A comparison of the BMV T=1 particles was made with the reassembled T=1 particles produced from the coat protein of trypsin treated alfalfa mosaic virus (AlMV), another bromovirus. There is little resemblance between the two particles. The BMV particle, with a maximum diameter of 195 A, is made from distinctive pentameric capsomeres with large holes along the 3-fold axis, while the AlMV particle, of approximate maximum diameter 220 A, has subunits closely packed around the 3-fold axis, large holes along the 5-fold axis, and few contacts within pentamers. In both particles crucial linkages are made about icosahedral dyads.

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Year:  2005        PMID: 15713465     DOI: 10.1016/j.jmb.2004.12.015

Source DB:  PubMed          Journal:  J Mol Biol        ISSN: 0022-2836            Impact factor:   5.469


  16 in total

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Authors:  Yurii G Kuznetsov; Min Zhang; Thomas M Menees; Alexander McPherson; Suzanne Sandmeyer
Journal:  J Virol       Date:  2005-07       Impact factor: 5.103

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3.  Geometric considerations in virus capsid size specificity, auxiliary requirements, and buckling.

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Journal:  Proc Natl Acad Sci U S A       Date:  2009-05-13       Impact factor: 11.205

4.  Vibrational dynamics of icosahedrally symmetric biomolecular assemblies compared with predictions based on continuum elasticity.

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Journal:  Biophys J       Date:  2009-06-03       Impact factor: 4.033

5.  An examination of the electrostatic interactions between the N-terminal tail of the Brome Mosaic Virus coat protein and encapsidated RNAs.

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Journal:  J Mol Biol       Date:  2012-04-01       Impact factor: 5.469

6.  The tripartite virions of the brome mosaic virus have distinct physical properties that affect the timing of the infection process.

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Journal:  Mol Plant Pathol       Date:  2016-08-14       Impact factor: 5.663

8.  Mechanisms of size control and polymorphism in viral capsid assembly.

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Journal:  Nano Lett       Date:  2008-10-25       Impact factor: 11.189

9.  Role of electrostatics in the assembly pathway of a single-stranded RNA virus.

Authors:  Rees F Garmann; Mauricio Comas-Garcia; Melissa S T Koay; Jeroen J L M Cornelissen; Charles M Knobler; William M Gelbart
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10.  Induction of particle polymorphism by cucumber necrosis virus coat protein mutants in vivo.

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Journal:  J Virol       Date:  2007-11-21       Impact factor: 5.103

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